Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Cells May Shoot Messenger To Halt Protein Production

21.05.2004


Scientists have found that living cells will sometimes “shoot the messenger” as a way to halt production of certain proteins



The study, published in the May 21 issue of the journal Molecular Cell, shows that cells sometimes destroy the chemical messages that contain information for making proteins even as the messages are being “read.” The work was done by scientists at The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute.

The findings describe a poorly understood biochemical mechanism that cells may use to suddenly stop producing proteins like growth factors that activate genes in response to a hormone or other signaling chemical. The mechanism also plays a key role in Cooley’s anemia, which causes the loss of red blood cells in infants and children, and may contribute to changes in gene activation in cancer.


The mechanism involves a recently discovered enzyme that destroys the ribbon-like molecules of messenger RNA (mRNA). Messenger RNA is a copy of gene, and it contains information that describes the structure of a protein. It carries that information from genes in the cell nucleus to the region of the cell where proteins are made.

“Controlling mRNA degradation is one of the key ways that cells regulate how much of a particular protein they produce,” says senior author Daniel R. Schoenberg, professor of molecular and cellular biochemistry. “The mechanism we describe is a completely new concept in the field.”

Proteins carry out most of the work in cells. Production of a protein begins when the gene carrying the information for a protein opens — the DNA unwinds — and the information is copied in the form of another molecule, mRNA.

Next, the mRNA leaves the cell nucleus and enters the cell cytoplasm. There, complexes known as ribosomes attach to one end of the mRNA.

The ribosomes then travel along the mRNA, reading the encoded genetic message as they go. That message describes the chain of amino acids needed to make that particular protein.

As each ribosome travels along the mRNA, it builds the protein by joining the next amino acid in the sequence. When it reaches the end, it releases the raw protein into the cytoplasm.

After making a protein, the mRNA is either reused to make more of its encoded protein, or it is destroyed. Scientists generally believe the mRNA destruction is carried out in multiple steps, beginning when one end of the mRNA is lopped off. The doomed molecule is then transported to nearby recycling complexes.

The current study, carried out by Feng Yang, a graduate student in the Ohio State Biochemistry Program, shows that some mRNAs are degraded through a quicker means: they are hit much earlier in the process.

The findings show that an enzyme Schoenberg previously discovered, known as PMR1 (polysomal ribonuclease 1), attaches to the mRNA of some proteins and chops the mRNA into pieces while ribosomes are reading it.

“The enzyme is sitting right there waiting to nail it, poised for someone to pull the pin on the hand grenade,” Schoenberg says. “That gives the cell tremendous flexibility when an mRNA needs to be degraded.”

This pathway works only on certain classes of mRNA, and Schoenberg now wants to learn how the enzyme identifies which mRNA molecules to join to, and to identify the signals that trigger PMR1 to destroy an mRNA.

A grant from the National Institutes of Health funded this research.

The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute encompasses six interdisciplinary research programs, over 200 investigators and the Arthur G. James Cancer Hospital and Richard J. Solove Research Institute. The OSU CCC-James is a founding member of the National Comprehensive Cancer Network, and The James is consistently ranked by U.S. News & World Report as one of America’s best cancer hospitals.

Darrell E. Ward | OSU
Further information:
http://researchnews.osu.edu/archive/rnadecay.htm

More articles from Life Sciences:

nachricht Hunting pathogens at full force
22.03.2017 | Helmholtz-Zentrum für Infektionsforschung

nachricht A 155 carat diamond with 92 mm diameter
22.03.2017 | Universität Augsburg

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Giant Magnetic Fields in the Universe

Astronomers from Bonn and Tautenburg in Thuringia (Germany) used the 100-m radio telescope at Effelsberg to observe several galaxy clusters. At the edges of these large accumulations of dark matter, stellar systems (galaxies), hot gas, and charged particles, they found magnetic fields that are exceptionally ordered over distances of many million light years. This makes them the most extended magnetic fields in the universe known so far.

The results will be published on March 22 in the journal „Astronomy & Astrophysics“.

Galaxy clusters are the largest gravitationally bound structures in the universe. With a typical extent of about 10 million light years, i.e. 100 times the...

Im Focus: Tracing down linear ubiquitination

Researchers at the Goethe University Frankfurt, together with partners from the University of Tübingen in Germany and Queen Mary University as well as Francis Crick Institute from London (UK) have developed a novel technology to decipher the secret ubiquitin code.

Ubiquitin is a small protein that can be linked to other cellular proteins, thereby controlling and modulating their functions. The attachment occurs in many...

Im Focus: Perovskite edges can be tuned for optoelectronic performance

Layered 2D material improves efficiency for solar cells and LEDs

In the eternal search for next generation high-efficiency solar cells and LEDs, scientists at Los Alamos National Laboratory and their partners are creating...

Im Focus: Polymer-coated silicon nanosheets as alternative to graphene: A perfect team for nanoelectronics

Silicon nanosheets are thin, two-dimensional layers with exceptional optoelectronic properties very similar to those of graphene. Albeit, the nanosheets are less stable. Now researchers at the Technical University of Munich (TUM) have, for the first time ever, produced a composite material combining silicon nanosheets and a polymer that is both UV-resistant and easy to process. This brings the scientists a significant step closer to industrial applications like flexible displays and photosensors.

Silicon nanosheets are thin, two-dimensional layers with exceptional optoelectronic properties very similar to those of graphene. Albeit, the nanosheets are...

Im Focus: Researchers Imitate Molecular Crowding in Cells

Enzymes behave differently in a test tube compared with the molecular scrum of a living cell. Chemists from the University of Basel have now been able to simulate these confined natural conditions in artificial vesicles for the first time. As reported in the academic journal Small, the results are offering better insight into the development of nanoreactors and artificial organelles.

Enzymes behave differently in a test tube compared with the molecular scrum of a living cell. Chemists from the University of Basel have now been able to...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

International Land Use Symposium ILUS 2017: Call for Abstracts and Registration open

20.03.2017 | Event News

CONNECT 2017: International congress on connective tissue

14.03.2017 | Event News

ICTM Conference: Turbine Construction between Big Data and Additive Manufacturing

07.03.2017 | Event News

 
Latest News

Pulverizing electronic waste is green, clean -- and cold

22.03.2017 | Materials Sciences

Astronomers hazard a ride in a 'drifting carousel' to understand pulsating stars

22.03.2017 | Physics and Astronomy

New gel-like coating beefs up the performance of lithium-sulfur batteries

22.03.2017 | Materials Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>