Sentences with phrase «many ribosomes»

Nowhere was he creating membranes, ribosomes, transmembrane proteins, enzymes etc etc etc from scratch.

This makes me happy: Research on ribosomes by Noller and others has led to the development of novel antibiotics that hold promise for use against drug - resistant bacteria.

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.

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.

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.

Having more ribosomes made the plants grow bigger.

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

«A new class of antibiotics to combat drug resistance: Newly discovered antibiotic binds to ribosome, disrupts protein synthesis.»

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

«As with some other ribosome groups, we have a friendly sense of rivalry.

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.

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.

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

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.

«All subsequent structures of the whole ribosome or other [large] subunits have depended on this structure» that Ban produced, «and it was a tour de force,» writes Ramakrishnan, who has never collaborated with Ban.

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.

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

Venkatraman Ramakrishnan, Thomas Steitz and Ada Yonath first determined how to image the ribosome, then revealed how it does its protein - making work

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.

These ribosomes may not build all kinds of proteins, instead opting to craft only specialty products.

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.

The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA).

That was surprising, he explains, because «fibrillarin resides deep within the nucleolus of the host cell... [where it] methylates ribosomal RNA molecules, which then go on to form ribosomes,» but its full function may not be completely understood.

Ribosomes join up the building blocks of proteins in cells.

Ribosomes, the cellular factories that manufacture proteins, contain both RNA and protein, but exactly how all of the different ribosomal components contribute to protein synthesis is still not clear.

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

«Under warmer temperatures, marine micro-algae do not seem to produce as many ribosomes as under lower temperatures.

Decoding of the genetic message involves both the ribosome and its tRNA substrates.

When Roberta peered through the microscope at samples from the fly, she was amazed to find mitochondria, ribosomes, muscle bands — and the nucleus, which houses the cell's genome.

The ability of RNA to orchestrate large - scale conformational changes may help explain why the ribosome and the spliceosome are RNA - based machines.

DNA is transcribed into messenger RNA (mRNA) that carries the code to ribosomes, the molecular machines that build proteins by reading the mRNA instructions.

Here we report the crystal structure of EF - P bound to the Thermus thermophilus 70S ribosome along with the initiator transfer RNA N - formyl - methionyl - tRNAi (fMet - tRNAifMet) and a short piece of messenger RNA (mRNA) at a resolution of 3.5 angstroms.

Individual polypeptide nascent chains can adopt distinct conformations within the ribosome exit tunnel.

Expression of the Escherichia coli tryptophanase operon depends on ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical.

Allan Jacobson, Ph.D., of the University of Massachusetts Medical School and co-founder of PTC Therapeutics, the company that developed ataluren, and David Bedwell, Ph.D., professor of the UAB Department of Biochemistry and Molecular Genetics, have sought to understand precisely how ataluren allows the ribosome, the machinery of cellular protein synthesis, to skip over these inserted stop signs and produce proteins that have normal or near - normal function.

Elongation factor P binds to the ribosome so as to position the initiator transfer RNA for the first bond formation.

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.

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.

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 protein assembly line consists of microtubules that serve as train tracks on which the raw materials — including messenger RNA (mRNA)-- are carried to the protein - making machinery, called ribosomes.

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.

Proteins are produced by ribosomes, and misfolding can occur if they stall while decoding a damaged template.

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.

Large protein complexes with RNA are found in the ribosome particles, which are in fact «ribozymes».

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.