Sentences with phrase «of ribosomes»

In particular, the rate of protein synthesis strongly increases under high temperatures even though the numbers of ribosomes and their associated rRNAs decreases.

Thus, at higher temperatures, eukaryotic phytoplankton seem to require a lower density of ribosomes to produce the required amounts of cellular protein.

Despite the intricacies of ribosomes, cells are able to churn out 100,000 of them every hour.

A segment of the 5» nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation.

The researchers were able to show that a reduction in the number of ribosomes — organelles known as the protein factories of the cell — is responsible for the disruption in the formation of red blood cells found in patients with DBA.

Investigations of how short chains of nucleic acids replicate themselves in vitro have even provided clues to primitive genetic codes for translating nucleic acid information into protein information, systems that could have preceded the elaborate machinery of ribosomes and activating enzymes with which cells now manufacture protein.

Gerton hypothesized that cancer cells, which are highly proliferative and might need more than the usual amount of ribosomes, would select for expansion of copy number.

It encodes structural components of ribosomes, the miniature factories responsible for producing the proteins that carry out many functions of the cell.

RNA acts as a messenger between DNA and the protein synthesis complexes known as ribosomes, forms vital portions of ribosomes, and acts as an essential carrier molecule for amino acids to be used in protein synthesis.

«The textbook view of ribosomes is that they are all the same,» Barna said.

Perhaps other biological processes are also controlled, in part, by having specific types of ribosomes build particular proteins, Barna said.

He and his group now plan to enhance still further the resolution attainable with their cryo - electron microscope, and will then use it to investigate the structures of ribosomes that have been brought to a halt by other chemical agents.

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.

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.

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.

These RNA copies can then used to direct protein synthesis, but they can also be used directly as parts of ribosomes or spliceosomes.

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.

degree prompted his desire to visualize the three - dimensional structure of ribosomes.

It seems that the fertilizer increased the number of ribosomes (tiny organelles in the non-nuclear part of the cell).

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.

At the next stage, RNA molecules began to synthesize proteins, first by developing RNA adaptor molecules that can bind activated amino acids and then by arranging them according to an RNA template using other RNA molecules such as the RNA core of the ribosome.

Steitz and Peter Moore, a biophysical chemist at Yale, had discussed using x-ray crystallography to solve the structure of the ribosome for years.

He decided to delay starting his own group for a year and a half, the time he estimated he needed to solve the structure of the ribosome.

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.

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.

Most studies on the details of this process have focused on the role of the ribosome.

It's fitting that this year's chemistry prize has been awarded to Venkatraman Ramakrishnan, who used the institute's # 95 million Swiss Light Source for his prize - winning studies on the structure of the ribosome.

We determined a 5.8 angstrom — resolution cryo — electron microscopy and single - particle reconstruction of a ribosome stalled during translation of the tnaC leader gene.

Noller (p. 1508) discusses how the basic building block of RNA — the double helix — has been fashioned into the intricate «protein - like» three - dimensional surfaces of the ribosome.

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.

The collaboratinggroups at the MPIB and LMU have now investigated the clearance of ribosome - blocked proteins destined for the mitochondria.

Steitz shared the 2009 chemistry Nobel for his elegant elucidation of the three - dimensional structure and detailed function of the ribosome, the cellular organelle charged with the actual production of proteins as per the instructions of the genetic code.

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.

The resistance gene, however, by changing the shape of the ribosome, succeeds in blocking the drug — but at the cost of slowing down protein output.

As a consequence, at a certain point during translation, the conformation of the ribosome's active site is distorted in such a way that further elongation of the nascent peptide becomes impossible.

Instead, the signal peptide adopts a specific conformation in the presence of the antibiotic, which blocks and inhibits the active center of the ribosome, thus accounting for the premature stop.

When the drug is present, it binds within the tunnel of the ribosome and interacts with the translating leader peptide to stall protein synthesis.

We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF - G in the posttranslocational state using the antibiotic fusidic acid.

Crystal structures of the ribosome bound to elongation factors provide insights into translocation and decoding.

In what many say is the scientific equivalent of scaling Mount Everest, researchers have figured out almost the entire structure of one part of the ribosome, the cell's giant protein factory.

Next they tested an additional 27 genes that are known to be involved in various steps of ribosome biogenesis to verify whether SSUP was required for ESC maintenance.

The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State

Joint winner of the 2009 chemistry prize with Thomas Steitz and Ada Yonath «for studies of the structure and function of the ribosome.»

Using the 58 eggs confiscated in the Folgosa case back in 2003, she and her team searched for short DNA sequences that coded for a piece of the ribosome, the cell's protein - producing factory.

«You'll see that the guy goes into the middle of the ribosome, and suddenly up comes a puff of smoke,» says Berg.

There are two sets of protein translation systems in mammalian cells — the cytoplasmic translation system and the mitochondrial translation system — both of which are composed of ribosome, tRNAs and translation factors.

The dance begins with a pile of 20 students in blue hospital gowns — representing the 30S subunit of the ribosome — oozing across the grass.

In her lecture today, Ada Yonath compared her scientific quest to determine the structure of the ribosome to a climb of the Mount Everest.

Researchers applied the findings to a mouse model with a genetic mutation in a component of the ribosome — the machinery that makes proteins — and the rate of protein production was reduced in stem cells by 30 percent.

Nobel Laureate Ada Yonath, who was awarded the 2009 Nobel Prize in Chemistry «for studies of the structure and function of the ribosome «with X-ray crystallography, is currently researching species - specific antibiotics.