Corporate Banner
Satellite Banner
Proteomics
Scientific Community
 
Become a Member | Sign in
Home>News>This Article
  News
Return

Ancient Enzymes Function like Nanopistons to Unwind RNA

Published: Wednesday, September 05, 2012
Last Updated: Wednesday, September 05, 2012
Bookmark and Share
Molecular biologists have solved one of the mysteries of how double-stranded RNA is remodeled inside cells in both their normal and disease states.

The discovery may have implications for treating cancer and viruses in humans.

The research, which was published this week in Nature, found that DEAD-box proteins, which are ancient enzymes found in all forms of life, function as recycling “nanopistons.”

They use chemical energy to clamp down and pry open RNA strands, thereby enabling the formation of new structures. This remodeling of RNA is essential to the basic functioning of cells.

“If you want to couple fuel energy to mechanical work to drive strand separation, this is a very versatile mechanism,” said co-author Alan Lambowitz, the Nancy Lee and Perry R. Bass Regents Chair in Molecular Biology in the College of Natural Sciences and director of the Institute for Cellular and Molecular Biology.

In all cellular organisms RNA (ribonucleic acid) plays a fundamental role in the translation of genetic information into the synthesis of proteins. DEAD-box proteins are the largest family of what are known as RNA helicases, which unwind RNA.

“It has been known for some time that these enzymes do not function like traditional helicases,” said Eckhard Jankowsky, professor of biochemistry at Case Western Reserve University Medical School.

“The research by Lambowitz and his colleagues now provides the critical information that explains how the unwinding reaction works. It marks a major step toward understanding the molecular mechanics for many steps in RNA biology.”

Lambowitz said that the basic insight came when Anna Mallam, a postdoctoral researcher in his lab, hypothesized that DEAD-box proteins function modularly. One area on the protein binds to an ATP molecule, which is the energy source. Another area binds to the double-stranded RNA.

“Once the second domain is latched on to the RNA,” said Mallam, “and the first has got its ATP, the ‘piston’ comes down. It has a sharp edge that drives between the two strands and also grabs on one strand and bends it out of the way.”

Lambowitz, Mallam and their colleagues uncovered this mechanism in Mss116p, a DEAD-box protein in yeast. The mechanism is almost certainly universal to the entire family of the proteins, however, and therefore to all domains of life.


“Every DEAD-box protein that we know about has the same structure,” said Lambowitz, “and they all presumably use the same mechanism.”


This flexibility of DEAD-box proteins is essential to the functioning of healthy cells, which rely on a range of RNA molecules for basic processes, including protein synthesis.


This flexibility is also hijacked in cancers — where over-expression of DEAD-box proteins may help drive uncontrolled cell proliferation — and in infections caused by bacteria, fungi and viruses, which rely on specific DEAD-box proteins for their propagation.


“These findings could have far-reaching implications for our ability to control the activities of proteins in this class when their functions go awry in disease states,” said Michael Bender, program director in the Division of Genetics and Developmental Biology at the National Institutes of Health, which partially funded the work.

Lambowitz even sees potential, much further down the line, for using the nanopistons as the basis of biomedical technology.


“You can even envision, in the far future, how they might be incorporated into artificial nanomachines,” he said, “for switches and other mechanical devices inside and outside the cell.”


Further Information

Join For Free

Access to this exclusive content is for Technology Networks Premium members only.

Join Technology Networks Premium for free access to:

  • Exclusive articles
  • Presentations from international conferences
  • Over 3,900+ scientific posters on ePosters
  • More than 5,300+ scientific videos on LabTube
  • 35 community eNewsletters


Sign In



Forgotten your details? Click Here
If you are not a member you can join here

*Please note: By logging into TechnologyNetworks.com you agree to accept the use of cookies. To find out more about the cookies we use and how to delete them, see our privacy policy.

Related Content

Supercomputing Tumor Suppression Protein Model
TACC/XSEDE's Stampede supercomputer simulates largest atomic level system to date.
Monday, October 31, 2016
Mechanism of Tumor Suppressing Gene Uncovered
The most commonly mutated gene in cancer,p53, works to prevent tumor formation by keeping mobile elements in check that otherwise lead to genomic instability, UT Southwestern Medical Center researchers have found.
Tuesday, January 26, 2016
Can Cell Cycle Protein Prevent or Kill Breast Cancer Tumors?
An MD Anderson study has shown the potential of a simple molecule involved in cancer metabolism as a powerful therapeutic.
Monday, July 20, 2015
Unique Peptide Could Treat Cancers, Neurological Disorders, Infectious Diseases
Scientists have synthesized a peptide that shows potential for pharmaceutical development through an ability to induce a cell-recycling process called autophagy.
Monday, February 18, 2013
Metabolic Protein Launches Sugar Feast that Nurtures Brain Tumors
PKM2 slips into nucleus to promote cancer; potential biomarker and drug approach discovered.
Wednesday, November 28, 2012
Researchers Identify New, Cancer-Causing Role for Protein
Key to Akt activation is ubiquitination by a surprising culprit - TRAF6.
Tuesday, September 01, 2009
New Genomic Technique Uncovers Coral Transcriptome
Researchers have uncovered the larval transcriptome of a reef-building coral by utilizing a new technique for cDNA preparation.
Tuesday, May 12, 2009
Protein Controls Aging by Controlling Insulin
The gene expresses a protein that works by repressing intracellular signals of insulin and insulin-like growth factor-1, and may function as an anti-aging hormone in mammals.
Friday, September 16, 2005
Scientific News
Top 10 Life Science Innovations of 2016
2016 has seen the release of some truly innovative products. To help you digest these developments, The Scientist have listed their top picks for the year.
Largest Resource of Protein-Protein Interactions
Researchers have developed the largest ever database of protein-protein interactions.
Bright Red Fluorescent Protein Created
Scientists have created a bright red, fluorescent protein that could be used to track essential cellular processes.
Protein Self-Regulates Abundance
Researchers have uncovered how a protein, that plays a crucial role in embryonic stem cell renewal, is regulated.
'Lab on the Skin' for Sweat Analysis
Northwestern University researchers develop a low-cost wearable electronic device that collects and analyzes sweat for health monitoring.
Building Better Nanodiscs
Researchers have improved upon the design of nanodiscs that provide an unprecedented view of viral infection.
Breast Cancer Cells Starve for Cystine
Depriving triple negative breast cancer, a treatment-resistant form of breast cancer, of cystine results in cancer cell death.
Novel Urine Test to Predict High-Risk Cervical Cancer
Preliminary studies affirm accuracy and potential cost savings to screen for virus-caused malignancy.
Protein-Folding Gene Helps Heal Wounds
Researchers identified a protein that dramatically accelerates wound healing in animal models.
Crop Yield Gets Boost with Modified Genes
Researchers increase plant proteins that result in more efficient use of sunlight.
Scroll Up
Scroll Down
Skyscraper Banner

SELECTBIO Market Reports
Go to LabTube
Go to eposters
 
Access to the latest scientific news
Exclusive articles
Upload and share your posters on ePosters
Latest presentations and webinars
View a library of 1,800+ scientific and medical posters
3,900+ scientific and medical posters
A library of 2,500+ scientific videos on LabTube
5,300+ scientific videos
Close
Premium CrownJOIN TECHNOLOGY NETWORKS PREMIUM FOR FREE!