Harvesting earthworms by a practice called 'worm grunting' is widespread in the Southeastern USA. The technique involves rhythmically scraping a wooden stake driven into the ground with a flat metal object.
A common assumption is that vibrations cause the worms to surface, but this phenomenon had not been studied.
We demonstrate that Diplocardia earthworms emerge from the soil within minutes following the onset of seismic vibrations caused by grunting.
The results are discussed in relation to two hypotheses: that worms are escaping vibrations caused by digging foragers, and that worms are surfacing in response to vibrations caused by falling rain.
Royal Society Journal Biology Letters
Biology Letters publishes short, innovative and cutting-edge research articles and opinion pieces accessible to scientists from across the biological sciences. The journal is characterised by stringent peer-review, rapid publication and broad dissemination of succinct high-quality research communications.
publishing.royalsociety/biologyletters
воскресенье, 24 апреля 2011 г.
Dual Enzymatic Activity Of RECQ1 Explained By Different Quaternary Structures
The transient opening of the DNA double helix is a fundamental step in several DNA metabolic processes. This reaction is driven by proteins called helicases, which make use of ATP as fuel to unwind the DNA duplex. The RecQ family of helicases helps maintain genome stability. Recent studies have shown that RecQ helicases, in addition to promoting DNA unwinding, can also catalyze the opposite reaction: the pairing of the partially unwound DNA duplexes. The mechanisms underlying the regulation of this dual enzymatic activity are unknown, however.
In a new study published online in the open access journal PLoS Biology, Laura Muzzolini, Alessandro Vindigni, and colleagues describe two structural forms of the human RECQ1 helicase, a large oligomeric complex composed of five or six subunits and a smaller form consistent with only one or two molecules. An initial view of the three-dimensional structure of the larger complex is provided, including a demonstration that this state is associated with DNA strand annealing, whereas the smaller form carries out DNA unwinding. The functional switch from strand-annealing to DNA unwinding is controlled by ATP binding, which promotes the dissociation of the larger, higher-order complexes. By providing insight into the mechanisms regulating RecQ helicase activity, this study opens a new window into a fundamental aspect of DNA metabolism.
Citation: Muzzolini L, Beuron F, Patwa rdhan A, Popuri V, Cui S, et al. (2007) Different quaternary structures of human RECQ1 are associated with its dual enzymatic activity.
PLoS Biol 5(2): e20. doi:10.1371/journal.pbio.0050020.
CONTACT:
Alessandro Vindigni
ICGEB
Padriciano 99
Trieste, TS 34012
Italy
PLEASE MENTION THE OPEN-ACCESS JOURNAL PLoS BIOLOGY (plosbiology/) AS THE SOURCE FOR THESE ARTICLES AND PROVIDE A LINK TO THE FREELY-AVAILABLE TEXT. THANK YOU.
All works published in PLoS Biology are open access. Everything is immediately available--to read, download, redistribute, include in databases, and otherwise use--without cost to anyone, anywhere, subject only to the condition that the original authorship and source are properly attributed. Copyright is retained by the authors. The Public Library of Science uses the Creative Commons Attribution License.
Contact: Natalie Bouaravong
Public Library of Science
In a new study published online in the open access journal PLoS Biology, Laura Muzzolini, Alessandro Vindigni, and colleagues describe two structural forms of the human RECQ1 helicase, a large oligomeric complex composed of five or six subunits and a smaller form consistent with only one or two molecules. An initial view of the three-dimensional structure of the larger complex is provided, including a demonstration that this state is associated with DNA strand annealing, whereas the smaller form carries out DNA unwinding. The functional switch from strand-annealing to DNA unwinding is controlled by ATP binding, which promotes the dissociation of the larger, higher-order complexes. By providing insight into the mechanisms regulating RecQ helicase activity, this study opens a new window into a fundamental aspect of DNA metabolism.
Citation: Muzzolini L, Beuron F, Patwa rdhan A, Popuri V, Cui S, et al. (2007) Different quaternary structures of human RECQ1 are associated with its dual enzymatic activity.
PLoS Biol 5(2): e20. doi:10.1371/journal.pbio.0050020.
CONTACT:
Alessandro Vindigni
ICGEB
Padriciano 99
Trieste, TS 34012
Italy
PLEASE MENTION THE OPEN-ACCESS JOURNAL PLoS BIOLOGY (plosbiology/) AS THE SOURCE FOR THESE ARTICLES AND PROVIDE A LINK TO THE FREELY-AVAILABLE TEXT. THANK YOU.
All works published in PLoS Biology are open access. Everything is immediately available--to read, download, redistribute, include in databases, and otherwise use--without cost to anyone, anywhere, subject only to the condition that the original authorship and source are properly attributed. Copyright is retained by the authors. The Public Library of Science uses the Creative Commons Attribution License.
Contact: Natalie Bouaravong
Public Library of Science
Key Step In Programmed Cell Death Uncovered By St. Jude Researchers
Investigators at St. Jude Children's Research Hospital have discovered a dance of proteins that protects certain cells from undergoing apoptosis, also known as programmed cell death. Understanding the fine points of apoptosis is important to researchers seeking ways to control this process.
In a series of experiments, St. Jude researchers found that if any one of three molecules is missing, certain cells lose the ability to protect themselves from apoptosis. A report on this work appears in the advance online publication of Nature.
"This is probably the first description of what is happening mechanistically that contributes to the ability of cells to delay apoptosis," said James Ihle, Ph.D., the paper's senior author and chair of the St. Jude Department of Biochemistry. "It provides incredible insights into how three proteins work and how they can control apoptosis."
The molecular interactions that St. Jude researchers describe in Nature play out in nerve cells and blood cells that develop from hematopoietic (blood-forming) stem cells.
A research team elsewhere recently reported that Kostmann's syndrome, a potentially fatal inherited deficiency of granulocytes in children, caused by excessive apoptosis of granulocytes, results from a deficiency in one of the three proteins, called Hax1.
"This suggests that the protein is playing basically the same role in humans as we described in mice," Ihle said.
Apoptosis rids the body of faulty or unneeded cells. However, molecular malfunctions that trigger apoptosis may cause some diseases, including Parkinson's disease. Understanding the biochemical interactions that control the extent of programmed cell death could lead to new treatments.
St. Jude biochemists have long studied how cytokines - small proteins used by neurons and blood-borne cells to communicate messages - contribute to keeping cells alive. For example, they demonstrated earlier that most cytokines controlling hematopoietic cells require an enzyme called Jak2, or Jak3 in lymphocytes, at the receptors where cytokines attached to the cell.
In screening for components that are regulated by the Jak enzymes, the St. Jude team found the Hax1 protein.
"That was intriguing because several studies suggested that Hax1 was controlled by cytokine signaling," Ihle said. "Also, studies have suggested that if you overexpressed Hax1 in cells, the cells were protected from undergoing apoptosis."
To pursue this lead, the researchers genetically engineered mice that lacked the gene for Hax1. The results showed that apoptosis in the animals' brain caused extensive nerve cell degeneration that killed the mice within 10 to 12 weeks. Second, apoptosis in immune-system lymphocytes occurred in the altered mice eight hours sooner than in those with the Hax1 gene, when limited amounts of cytokines were available.
"That additional window of survival is extremely important because in the body, cytokines are limiting." Ihle said. "The key observation was that Hax1 was important in helping cells to survive. Importantly, what happened to the mice we generated was remarkably similar to what happens if you remove the mitochondrial enzymes called HtrA2 or Parl."
Exploring the similarities, the investigators found that Hax1 and Parl pair up in the inner membrane of the mitochondria - tiny chemical packets that serve as the main energy source for cells. HtrA2 is made in the cell's cytoplasm and is transported into the mitochondria, where the enzyme must have a region removed for it to be active. This requires snipping away 133 amino acids, the building blocks of proteins. The St. Jude researchers demonstrated that it is the Hax1/Parl pair that positions HtrA2 to allow the precise snipping that is required. Without Hax1, the snipping does not occur and HtrA2 remains inert.
In lymphocytes, members of the Bcl-2 family of proteins both protect and initiate apoptosis. For this reason, Ihle and the researchers explored this family of proteins to understand why lymphocytes needed an active HtrA2 mitochondrial enzyme. This led them to discover that if active HtrA2 were present, the incorporation of a protein called Bax into the mitochondrial outer membrane did not occur. This was significant since accumulation of Bax in the outer mitochondrial membrane allows the release of proteins that set off a chain of biochemical reactions, including the activation of enzymes that are responsible for cell death.
Other authors of this study include Jyh-Rong Chao, Kelli Boyd, Evan Parganas, Cheol Yi Hong and Joseph T. Opferman (all St. Jude).
This work was supported in part by grants from the National Institutes of Health and ALSAC.
St. Jude Children's Research Hospital
St. Jude Children's Research Hospital is internationally recognized for its pioneering work in finding cures and saving children with cancer and other catastrophic diseases. Founded by late entertainer Danny Thomas and based in Memphis, Tenn., St. Jude freely shares its discoveries with scientific and medical communities around the world. No family ever pays for treatments not covered by insurance, and families without insurance are never asked to pay. St. Jude is financially supported by ALSAC, its fundraising organization. For more information, please visit stjude/.
Source: Carrie Strehlau
St. Jude Children's Research Hospital
In a series of experiments, St. Jude researchers found that if any one of three molecules is missing, certain cells lose the ability to protect themselves from apoptosis. A report on this work appears in the advance online publication of Nature.
"This is probably the first description of what is happening mechanistically that contributes to the ability of cells to delay apoptosis," said James Ihle, Ph.D., the paper's senior author and chair of the St. Jude Department of Biochemistry. "It provides incredible insights into how three proteins work and how they can control apoptosis."
The molecular interactions that St. Jude researchers describe in Nature play out in nerve cells and blood cells that develop from hematopoietic (blood-forming) stem cells.
A research team elsewhere recently reported that Kostmann's syndrome, a potentially fatal inherited deficiency of granulocytes in children, caused by excessive apoptosis of granulocytes, results from a deficiency in one of the three proteins, called Hax1.
"This suggests that the protein is playing basically the same role in humans as we described in mice," Ihle said.
Apoptosis rids the body of faulty or unneeded cells. However, molecular malfunctions that trigger apoptosis may cause some diseases, including Parkinson's disease. Understanding the biochemical interactions that control the extent of programmed cell death could lead to new treatments.
St. Jude biochemists have long studied how cytokines - small proteins used by neurons and blood-borne cells to communicate messages - contribute to keeping cells alive. For example, they demonstrated earlier that most cytokines controlling hematopoietic cells require an enzyme called Jak2, or Jak3 in lymphocytes, at the receptors where cytokines attached to the cell.
In screening for components that are regulated by the Jak enzymes, the St. Jude team found the Hax1 protein.
"That was intriguing because several studies suggested that Hax1 was controlled by cytokine signaling," Ihle said. "Also, studies have suggested that if you overexpressed Hax1 in cells, the cells were protected from undergoing apoptosis."
To pursue this lead, the researchers genetically engineered mice that lacked the gene for Hax1. The results showed that apoptosis in the animals' brain caused extensive nerve cell degeneration that killed the mice within 10 to 12 weeks. Second, apoptosis in immune-system lymphocytes occurred in the altered mice eight hours sooner than in those with the Hax1 gene, when limited amounts of cytokines were available.
"That additional window of survival is extremely important because in the body, cytokines are limiting." Ihle said. "The key observation was that Hax1 was important in helping cells to survive. Importantly, what happened to the mice we generated was remarkably similar to what happens if you remove the mitochondrial enzymes called HtrA2 or Parl."
Exploring the similarities, the investigators found that Hax1 and Parl pair up in the inner membrane of the mitochondria - tiny chemical packets that serve as the main energy source for cells. HtrA2 is made in the cell's cytoplasm and is transported into the mitochondria, where the enzyme must have a region removed for it to be active. This requires snipping away 133 amino acids, the building blocks of proteins. The St. Jude researchers demonstrated that it is the Hax1/Parl pair that positions HtrA2 to allow the precise snipping that is required. Without Hax1, the snipping does not occur and HtrA2 remains inert.
In lymphocytes, members of the Bcl-2 family of proteins both protect and initiate apoptosis. For this reason, Ihle and the researchers explored this family of proteins to understand why lymphocytes needed an active HtrA2 mitochondrial enzyme. This led them to discover that if active HtrA2 were present, the incorporation of a protein called Bax into the mitochondrial outer membrane did not occur. This was significant since accumulation of Bax in the outer mitochondrial membrane allows the release of proteins that set off a chain of biochemical reactions, including the activation of enzymes that are responsible for cell death.
Other authors of this study include Jyh-Rong Chao, Kelli Boyd, Evan Parganas, Cheol Yi Hong and Joseph T. Opferman (all St. Jude).
This work was supported in part by grants from the National Institutes of Health and ALSAC.
St. Jude Children's Research Hospital
St. Jude Children's Research Hospital is internationally recognized for its pioneering work in finding cures and saving children with cancer and other catastrophic diseases. Founded by late entertainer Danny Thomas and based in Memphis, Tenn., St. Jude freely shares its discoveries with scientific and medical communities around the world. No family ever pays for treatments not covered by insurance, and families without insurance are never asked to pay. St. Jude is financially supported by ALSAC, its fundraising organization. For more information, please visit stjude/.
Source: Carrie Strehlau
St. Jude Children's Research Hospital
Caliper Life Sciences Develops Customized Transfection System For Boehringer Ingelheim
Caliper Life
Sciences, Inc. (Nasdaq: CALP), an established leader in the field of
robotics, is working with the pharmaceutical industry to develop customized
robotic transfection systems for protein expression. Caliper recently
created a unique solution for Boehringer Ingelheim that automates aspects
of Baculovirus expression.
To develop the system for Boehringer Ingelheim, Caliper's Integrated
Systems Group (ISG) worked directly with researchers to understand the
company's specific needs for each step of the Baculovirus expression
process. Caliper then utilized its expertise in the field of laboratory
automation and robotics to integrate its Sciclone(R) liquid handler along
with technology from third-party vendors to create a Staccato(R) laboratory
system that is reliable, effective and individualized.
Caliper's ISG team, a dedicated team of engineers and scientists with
experience in mechanical and electrical engineering, software development,
assay development and project management expertise, work closely with
customers to design and build each system according to specific needs.
"The capability to develop highly reliable integrated systems
illustrates our commitment to laboratory automation and robotics, and to
providing the pharmaceutical industry with innovative research tools that
meet unique needs," said Kevin Keras, Business Unit Manager, Integrated
Systems, Caliper Life Sciences. "We are dedicated to improving the workflow
for drug discovery and development and see tremendous value in partnering
with leading system providers to create solutions that incorporate a broad
range of capabilities."
About Caliper Life Sciences
Caliper Life Sciences is a leading provider of cutting-edge
technologies enabling researchers in the life sciences to create
life-saving and enhancing medicines and diagnostic tests more quickly and
efficiently. Caliper is aggressively innovating new technology to bridge
the gap between in vitro assays and in vivo results and then translate
those results into cures for human disease. Caliper's portfolio of
offerings includes state-of-the-art microfluidics, lab automation & liquid
handling, optical imaging technologies, and discovery & development
outsourcing solutions. For more information please visit
caliperLS.
Caliper, Sciclone and Staccato are registered trademarks of Caliper
Life Sciences, Inc.
Caliper Life Sciences, Inc
caliperLS
Sciences, Inc. (Nasdaq: CALP), an established leader in the field of
robotics, is working with the pharmaceutical industry to develop customized
robotic transfection systems for protein expression. Caliper recently
created a unique solution for Boehringer Ingelheim that automates aspects
of Baculovirus expression.
To develop the system for Boehringer Ingelheim, Caliper's Integrated
Systems Group (ISG) worked directly with researchers to understand the
company's specific needs for each step of the Baculovirus expression
process. Caliper then utilized its expertise in the field of laboratory
automation and robotics to integrate its Sciclone(R) liquid handler along
with technology from third-party vendors to create a Staccato(R) laboratory
system that is reliable, effective and individualized.
Caliper's ISG team, a dedicated team of engineers and scientists with
experience in mechanical and electrical engineering, software development,
assay development and project management expertise, work closely with
customers to design and build each system according to specific needs.
"The capability to develop highly reliable integrated systems
illustrates our commitment to laboratory automation and robotics, and to
providing the pharmaceutical industry with innovative research tools that
meet unique needs," said Kevin Keras, Business Unit Manager, Integrated
Systems, Caliper Life Sciences. "We are dedicated to improving the workflow
for drug discovery and development and see tremendous value in partnering
with leading system providers to create solutions that incorporate a broad
range of capabilities."
About Caliper Life Sciences
Caliper Life Sciences is a leading provider of cutting-edge
technologies enabling researchers in the life sciences to create
life-saving and enhancing medicines and diagnostic tests more quickly and
efficiently. Caliper is aggressively innovating new technology to bridge
the gap between in vitro assays and in vivo results and then translate
those results into cures for human disease. Caliper's portfolio of
offerings includes state-of-the-art microfluidics, lab automation & liquid
handling, optical imaging technologies, and discovery & development
outsourcing solutions. For more information please visit
caliperLS.
Caliper, Sciclone and Staccato are registered trademarks of Caliper
Life Sciences, Inc.
Caliper Life Sciences, Inc
caliperLS
The Oldest Ancestor Genome?
The origins of life represent a fascinating problem that has been
addressed using different approaches and a wide variety of technologies. A
theoretical approach consists of inferring a possible oldest ancestor
genome from a well-defined comparison of current ones. Mushegian and
Koonin did
this in 1996, creating a hypothetical Minimal Gene Set (MGS). In this new
paper from PLoS Computational Biology, Davide Chiarugi, Pierpaolo Degano,
and Roberto Marangoni, from the universities of Siena and Pisa, prove that
this MGS would not have been able support life.
One of the difficulties of such a hypothetical genome is validating it as
a functional biological system. The direct solution of synthesizing such a
genome in a laboratory is often extremely difficult, due to the great
complexity of a biological cell. In this paper, the authors present an
approach
for evaluating the chances a hypothetical organism has to be really
viable, relying on computer simulations.
The authors assumed the two conditions of reaching equilibrium and
producing biomass to be essential for an organism to live. The previous
MGS-prokaryote clearly does not express these qualities, but by adding new
genes and changing some of the previous ones, the authors managed to
produce a genome which adhered to their criteria of life - Virtual Cell
(ViCe). This is some 60 genes smaller than the MGS, and demonstrates
qualities similar to those seen in live bacteria, therefore indicating,
that this, in fact, could be the oldest ancestor genome.
A previous version of this article appeared as an Early Online Release on
July 26, 2007 (doi:10.1371/journal.pcbi.0030174.eor).
Please click here.
CITATION: Chiarugi D, Degano P, Marangoni R (2007) A computational
approach to the functional screening of genomes. PLoS Comput Biol 3(9):
e174.
doi:10.1371/journal.pcbi.0030174
About PLoS Computational Biology
PLoS Computational Biology features works of
exceptional significance that further our understanding of living systems
at all
scales through the application of computational methods. All works
published in PLoS Computational Biology are open access. Everything is
immediately
available subject only to the condition that the original authorship and
source are properly attributed. Copyright is retained by the authors. The
Public Library of Science uses the Creative Commons Attribution License.
About the Public Library of Science
The Public Library of Science (PLoS) is a non-profit organization of
scientists and physicians committed to making the world's scientific and
medical
literature a freely available public resource.
Public Library of Science.
185 Berry Street, Suite 3100
San Francisco, CA 94107
USA
addressed using different approaches and a wide variety of technologies. A
theoretical approach consists of inferring a possible oldest ancestor
genome from a well-defined comparison of current ones. Mushegian and
Koonin did
this in 1996, creating a hypothetical Minimal Gene Set (MGS). In this new
paper from PLoS Computational Biology, Davide Chiarugi, Pierpaolo Degano,
and Roberto Marangoni, from the universities of Siena and Pisa, prove that
this MGS would not have been able support life.
One of the difficulties of such a hypothetical genome is validating it as
a functional biological system. The direct solution of synthesizing such a
genome in a laboratory is often extremely difficult, due to the great
complexity of a biological cell. In this paper, the authors present an
approach
for evaluating the chances a hypothetical organism has to be really
viable, relying on computer simulations.
The authors assumed the two conditions of reaching equilibrium and
producing biomass to be essential for an organism to live. The previous
MGS-prokaryote clearly does not express these qualities, but by adding new
genes and changing some of the previous ones, the authors managed to
produce a genome which adhered to their criteria of life - Virtual Cell
(ViCe). This is some 60 genes smaller than the MGS, and demonstrates
qualities similar to those seen in live bacteria, therefore indicating,
that this, in fact, could be the oldest ancestor genome.
A previous version of this article appeared as an Early Online Release on
July 26, 2007 (doi:10.1371/journal.pcbi.0030174.eor).
Please click here.
CITATION: Chiarugi D, Degano P, Marangoni R (2007) A computational
approach to the functional screening of genomes. PLoS Comput Biol 3(9):
e174.
doi:10.1371/journal.pcbi.0030174
About PLoS Computational Biology
PLoS Computational Biology features works of
exceptional significance that further our understanding of living systems
at all
scales through the application of computational methods. All works
published in PLoS Computational Biology are open access. Everything is
immediately
available subject only to the condition that the original authorship and
source are properly attributed. Copyright is retained by the authors. The
Public Library of Science uses the Creative Commons Attribution License.
About the Public Library of Science
The Public Library of Science (PLoS) is a non-profit organization of
scientists and physicians committed to making the world's scientific and
medical
literature a freely available public resource.
Public Library of Science.
185 Berry Street, Suite 3100
San Francisco, CA 94107
USA
How Disruption Of Spectrin-Actin Network Causes Lens Cells In The Eye To Lose Shape
A network of proteins underlying the plasma membrane keeps epithelial cells in shape and maintains their orderly hexagonal packing in the mouse lens, say Nowak et al. The study will appear in the September 21, 2009 issue of the Journal of Cell Biology (online September 14).
Spectrin, F-actin, and associated proteins form a meshwork that supports and shapes the plasma membrane of red blood cells. A similar network underlies the membranes of other cell types, including lens fiber cells: elongated epithelial cells that encircle vertebrate lenses in concentric layers, appearing in cross section as tightly packed hexagons. Actin filaments within this membrane skeleton are stabilized by their association with members of the tropomyosin and tropomodulin families of actin-binding proteins.
In mice lacking tropomodulin1, gamma-tropomyosin was also lost from the membrane skeleton of lens fiber cells. F-actin and spectrin remained associated with the cell membrane, but gaps appeared in the usually continuous protein network, suggesting that the two actin-binding proteins stabilize a subset of actin filaments required to link the network together. Scanning electron microscopy revealed that fiber cell membrane protrusions, which interlock with neighboring cells, were distorted and irregularly arranged in the absence of tropomodulin1. And although the fiber cells appeared hexagonal when first forming at the lens' equator, they often became misshapen and disorganized as they matured and moved toward the lens' center.
Senior author Velia Fowler thinks that disruption of the spectrin-actin network alters the adhesive interactions between neighboring cells, causing their shapes and packing to become disordered in response to the mechanical stresses associated with lens growth and eye movements.
Source:
Rita Sullivan
Rockefeller University Press
Spectrin, F-actin, and associated proteins form a meshwork that supports and shapes the plasma membrane of red blood cells. A similar network underlies the membranes of other cell types, including lens fiber cells: elongated epithelial cells that encircle vertebrate lenses in concentric layers, appearing in cross section as tightly packed hexagons. Actin filaments within this membrane skeleton are stabilized by their association with members of the tropomyosin and tropomodulin families of actin-binding proteins.
In mice lacking tropomodulin1, gamma-tropomyosin was also lost from the membrane skeleton of lens fiber cells. F-actin and spectrin remained associated with the cell membrane, but gaps appeared in the usually continuous protein network, suggesting that the two actin-binding proteins stabilize a subset of actin filaments required to link the network together. Scanning electron microscopy revealed that fiber cell membrane protrusions, which interlock with neighboring cells, were distorted and irregularly arranged in the absence of tropomodulin1. And although the fiber cells appeared hexagonal when first forming at the lens' equator, they often became misshapen and disorganized as they matured and moved toward the lens' center.
Senior author Velia Fowler thinks that disruption of the spectrin-actin network alters the adhesive interactions between neighboring cells, causing their shapes and packing to become disordered in response to the mechanical stresses associated with lens growth and eye movements.
Source:
Rita Sullivan
Rockefeller University Press
Genome Research Published In The Latest Issue Of Science
Martin H. Spalding, professor and chair of the department of genetics, development and cell biology at Iowa State, is part of an international research team whose work is published in the journal Science.
The researchers sequenced and annotated the genome of the green algae chlamydomonas, a single-celled alga that has traits from both animals and plants.
"There may be lots of uses that come out of this, including basic bio-medical research, agricultural research, understanding certain diseases, learning more about photosynthesis, photosynthetic hydrogen production and many other areas," said Spalding.
Sequencing and annotating the genome took more than four years. Spalding's part of the research focused on his specialty, metabolism.
The chlamydomonas organism was chosen to be sequenced for several reasons.
It is a bridging species connecting back to when plants and animals began their evolutionary separation, so it contains traits of both. It produces chlorophyll and also flagella to help it move.
Another reason the alga was sequenced is that it is both a simple organism and a classic genetic model organism.
"It is such a simple system with a single-cell and straight-forward genetics," said Spalding. The project entailed sequencing the organism's 120 million nucleotides, as well as decoding the nucleotide sequence to identify the approximately 15,000 proteins coded by the genome.
Spalding hopes that further positive research will result from this work.
"It will be available for anyone to access," said Spalding, "and there may be lots of uses that we don't know yet."
Source: Martin Spalding
Iowa State University
The researchers sequenced and annotated the genome of the green algae chlamydomonas, a single-celled alga that has traits from both animals and plants.
"There may be lots of uses that come out of this, including basic bio-medical research, agricultural research, understanding certain diseases, learning more about photosynthesis, photosynthetic hydrogen production and many other areas," said Spalding.
Sequencing and annotating the genome took more than four years. Spalding's part of the research focused on his specialty, metabolism.
The chlamydomonas organism was chosen to be sequenced for several reasons.
It is a bridging species connecting back to when plants and animals began their evolutionary separation, so it contains traits of both. It produces chlorophyll and also flagella to help it move.
Another reason the alga was sequenced is that it is both a simple organism and a classic genetic model organism.
"It is such a simple system with a single-cell and straight-forward genetics," said Spalding. The project entailed sequencing the organism's 120 million nucleotides, as well as decoding the nucleotide sequence to identify the approximately 15,000 proteins coded by the genome.
Spalding hopes that further positive research will result from this work.
"It will be available for anyone to access," said Spalding, "and there may be lots of uses that we don't know yet."
Source: Martin Spalding
Iowa State University
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