Sentences with phrase «in ribosome»

Based on the degree of variation in this ribosome gene sequence, they estimate that the water contains 3,931 species or groups of species, the team reports today in the journal Nature.
NOP2 and PPRC1 are involved in ribosomal biogenesis and are coexpressed with DKC1, a gene involved in ribosome biogenesis and also a component of the telomerase ribonucleoprotein enzyme complex.
Read an obituary relating his breakthroughs in ribosome research.
This study reveals a new function for Hfq in ribosome biogenesis with implications for translational control.
And curious as to how widespread this phenomenon might be, the researchers looked for protein families with nearly identical members that are encoded by different genes and had significant variations in ribosome density across the family.
Getting at a mechanism for how DNA sequence could influence protein function, the researchers found that ribosomes density on β - actin RNA is more than a thousand times higher than on γ - actin RNA, and indeed all six actin genes had differences in ribosome density.
The domains of its RNAs all have irregular shapes and fit together in the ribosome like the pieces of a three - dimensional jigsaw puzzle to form a large, monolithic structure.
Large protein complexes with RNA are found in the ribosome particles, which are in fact «ribozymes».
As a result, once the protein has been manufactured in the ribosomes, the completed protein can not be released.
The researchers were also able to show that the process of translating certain sections of genetic information into new proteins is impaired in these ribosomes.
This work was quickly followed by evidence intimating the existence of a class of RNA in ribosomes that hybridized uniquely to genomic DNA of the same species, but not to that of foreign species (10), what later came to be known as mRNA.
Andrei Korostelev of the University of Massachusetts Medical School focuses on capturing minute structural changes in ribosomes as they translate RNA into proteins.
Kennedy is interested in understanding why reduced gene expression in ribosomes enhances longevity in yeast and worms — ribosomes are tiny organelles that occur within the cell and are involved in the production of proteins.

Not exact matches

A ribosome forms itself (we know not how), and even after being separated into its protein components in various chemicals, will jump back into working shape again when the chemicals are removed.
This additional dose of ribosomes was passed on in the cells of pollen and ovules to subsequent generations through the non-nuclear part of the cell.
It seems that the fertilizer increased the number of ribosomes (tiny organelles in the non-nuclear part of the cell).
So for a postdoc to want to take this on at that stage was remarkable,» Venki Ramakrishnan, a ribosome researcher at the MRC Laboratory of Molecular Biology in Cambridge, U.K., writes in an e-mail.
Ban and Poul Nissen, a membrane protein researcher at the Aarhus University in Denmark who was also doing a postdoc in Steitz's lab at the time, pushed to determine the structure of the large subunit of the ribosome at high resolution.
The scientists further discovered that whenever food enters the bowels, cells in the intestinal lining immediately respond by increasing the production of ribosomes, particularly in the food - facing part of the cell.
Ban chose to work on one of the most difficult problems in structural biology: imaging the active site of the ribosome, a site within the large subunit of the ribosome where the bonding of individual amino acids into a protein chain is catalyzed.
The 2009 Nobel Prize in Chemistry goes to Venkatraman Ramakrishnan, Thomas Steitz and Ada Yonath for studies of the protein - manufacturing ribosome, with implications for antibiotic development.
Thus RNA self - splicing can occur at a rate sufficient to support gene expression in a prokaryote, despite the likely presence of ribosomes on the nascent RNA.
Ribosomes join up the building blocks of proteins in cells.
They all use RNA molecules as messengers to transfer the information from DNA to cellular factories called ribosomes, which then build proteins, which in turn drive our metabolisms and form the structures of our cells.
Based on the ribosome profiling data, the researchers looked for genes that were being expressed differently in the trained mice, identifying 104 genes in total.
And with many large, complicated molecules found in and around cells — uch as ribosomes, which turn genetic instructions into working proteins — scientists simply could not make that happen.
The prize will be equally split between biophysicist Venkatraman Ramakrishnan of the MRC Laboratory of Molecular Biology in Cambridge in England, biochemist Thomas Steitz of Yale University and molecular biologist Ada Yonath of the Weizmann Institute of Science in Rehovot, Israel, for their work in using x-ray crystallography to get a precise, atomic - scale map of the ribosome — the protein - making machine in all cells with nuclei that makes life possible.
If the necessary ribosome - associated quality control machinery (RQC) does not function properly, defective proteins accumulate and form toxic aggregates in the cytoplasm of the cells.
Sofar, studies have focused on how the RQC recognizes and clears blocked ribosomes in the cytosol.
To begin to answer that question, the researchers modeled different combinations of promoters and ribosome - binding sites, finding that they could predict about 70 percent of the variance in the combinations.
This marks the second time in four years that the chemistry Nobel has been awarded to someone working with x-ray crystallography; in 2006 Roger Kornberg took the prize for detailing the structure of messenger RNA, which is the molecule that carries the information the ribosome uses to build proteins, such as insulin or hemoglobin.
The key to that is x-ray crystallography in which x-rays are shone through a crystal filled with ribosomes, creating a scatter pattern that reveals their inner workings (detected by CCDs, the inventors of which were honored yesterday with the 2009 Nobel in Physics).
And, although the ribosome is clearly in the realm of biology, its workings are pure chemistry, says chemist Thomas Lane, president of the American Chemical Society.
The pilot project tested a dozen or so of the most commonly used gene promoters (regions of DNA that facilitate gene transcription) and segments of DNA that encode ribosome - binding sites (sequences of messenger RNA that control protein translation) to determine whether they behave consistently in different cellular contexts.
The latest such roster — 271 proteins identified in a compartment of the cell nucleus called the nucleolus — is a first step toward fully deciphering this organelle, a critical element in the construction of ribosomes, which build proteins.
The team knew that the frequency and placement of the modified nucleosides in the strand changed how it folded, and hence how it interacted with the ribosome.
But findings in Moore's lab supported the view that mRNA strands with more of the nucleosides that tend to form tight bonds are, in fact, easier for ribosomes to translate.
Despite all these novel properties, Pandoraviruses display the essential characteristics of other viruses in that they contain no ribosome, produce no energy and do not divide.
When prompted, the tRNA synthetase charges a tRNA with the bio-orthogonal amino acid, which is then used by ribosomes to insert the tag into proteins made in the cell.
By taking a sort of molecular snapshot of an astrocyte's ribosomes, it's possible to see all the mRNA copies in progress and thus know which genes are active.
«Among other things, the ribosome is an expensive machine that the cell has invested a lot of energy in making, and now it's stuck on an mRNA.
However, if exercise restores or prevents deterioration of mitochondria and ribosomes in muscle cells, there's a good chance it does so in other tissues, too.
The same agents that damage DNA also damage its sister molecule messenger RNA (mRNA), which ferries transcripts of the genes to the tens of thousands of ribosomes in each cell.
And in fact it very well might be that once the ribosomes cease functioning properly, then anything can cause bees to go under.»
A study in the Proceedings of the National Academy of Sciences by May Berenbaum and colleagues finds that bee colony collapse disorder seems to be related to bees» ribosomes breaking down, which keeps them from making the proteins they need to deal with stress and disease.
«We couldn't look at ribosomes in the extracts,» Simms said, «but we could look at the proteins they made.
One of the defects is an error in mouse t - RNA (another type of RNA involved in translation) that stalls the ribosome and the other is a defect in the system that rescues the ribosome when it stalls.
And May Berenbaum, entomologist at the University of Illinois at Urbana - Champaign, talks about the latest publication related to colony collapse disorder and ribosome damage in the Proceedings of the National Academy of Sciences.
If the yeast's ribosomes jammed on the oxidized mRNA but were rescued by no - go decay, very little damaged mRNA would accumulate in the cell.
Its appearance following starvation and other stresses is associated with changes in the expression of over 500 genes, most prominently genes for the structural RNAs that are components of the ribosome — the enzyme responsible for protein synthesis.
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