Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:


RRF Recycles Form, Not Exact Function


Ribosome Recycling Factor Mimics Shape, But Not The Functions of Transfer RNA

RRF Protein Offers Potential Target for New Antibiotics

The fact that ribosome recycling factor (RRF) looks a lot like transfer RNA (tRNA) has not been lost on scientists. After all, both molecules are an important part of a bacteria’s ability to create new proteins. Researchers at the University of Pennsylvania School of Medicine and the University of Southern California, Santa Cruz, however, have found that this case of molecular mimicry has more to do with the shape of the molecules and not necessarily the job they perform. Their structural analysis of the RRF ribosome complex, presented in the current issue of the journal Cell, shows that RRF does not bind to the ribosome in the same location as tRNA.

"It is said that form follows function, but we see here that is not always true," said Akira Kaji, PhD, from Penn’s Department of Microbiology. "The L-shaped structure of both RRF and tRNA may have more to do with the spatial constraints of maneuvering within the folds of the ribosome than their actual tasks."

The actual task of the ribosome recycling factor has been something of a mystery for researchers. Until recently, science was unaware of its role in the process of creating proteins - and its potential as a target for new antibiotics.

Protein manufacture is a fundamental process of life that has been understood better in concept than in mechanics. While the DNA may encode the blueprints used to create proteins, it is the ribosome - an organelle within the cell - that actually builds a new protein.

There are three steps that are generally considered part of the scientific dogma surrounding the creation of new proteins: Initiation (the start of building a protein from messenger RNA that has been transcribed from DNA); Elongation (adding new amino acids to chain that becomes the protein via tRNA); and Termination (capping the amino acid chain off, so that it can be folded into a protein).

"There is one more crucial step that we had missed for a long time: recycling," said Kaji. It is the step where the machinery of the protein synthesis is "recycled" so that they can be used for the next round of protein synthesis. This step does not happen by magic, and we have to ask - How do you disassemble the complex of the protein synthesis machinery so that they can be used again for the next round of translation?

According to Kaji and his colleagues, RRF binds to different locations within the ribosomal complex at different times. It seems that, if the ribosome is the protein factory, the RRF is the foreman, moving from location to location to ’supervise’ the end of the assembly line. When the new protein is completed, RRF works in conjunction with other proteins to disassemble the ribosomal complex so that the components of the machinery are ready for the next round of protein creation.

Kaji believes that, since RRF plays the key role only in bacteria and mitochondria, the bacterial protein also provides an interesting target for new types of anti-bacterial agents. His research has already shown in the laboratory that bacteria lacking RRF cannot exist because of their inability to create new proteins.

"As bacteria mutate to become resistant to antibiotics, we must keep targeting parts of bacteria that are integral for functioning so that bacteria can not out-evolve antibiotics," said Kaji. "We are considering RRF as the target of a new type of antibiotic, an inhibitor of RRF that we can easily alter as bacteria become resistant."

Other scientists contributing to the research presented in Cell include Michael C. Kiel of Penn and Laura Lancaster and Harry F. Noller of the University of California at Santa Cruz.

Greg Lester | EurekAlert!
Further information:

More articles from Life Sciences:

nachricht Novel mechanisms of action discovered for the skin cancer medication Imiquimod
21.10.2016 | Technische Universität München

nachricht Second research flight into zero gravity
21.10.2016 | Universität Zürich

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: New 3-D wiring technique brings scalable quantum computers closer to reality

Researchers from the Institute for Quantum Computing (IQC) at the University of Waterloo led the development of a new extensible wiring technique capable of controlling superconducting quantum bits, representing a significant step towards to the realization of a scalable quantum computer.

"The quantum socket is a wiring method that uses three-dimensional wires based on spring-loaded pins to address individual qubits," said Jeremy Béjanin, a PhD...

Im Focus: Scientists develop a semiconductor nanocomposite material that moves in response to light

In a paper in Scientific Reports, a research team at Worcester Polytechnic Institute describes a novel light-activated phenomenon that could become the basis for applications as diverse as microscopic robotic grippers and more efficient solar cells.

A research team at Worcester Polytechnic Institute (WPI) has developed a revolutionary, light-activated semiconductor nanocomposite material that can be used...

Im Focus: Diamonds aren't forever: Sandia, Harvard team create first quantum computer bridge

By forcefully embedding two silicon atoms in a diamond matrix, Sandia researchers have demonstrated for the first time on a single chip all the components needed to create a quantum bridge to link quantum computers together.

"People have already built small quantum computers," says Sandia researcher Ryan Camacho. "Maybe the first useful one won't be a single giant quantum computer...

Im Focus: New Products - Highlights of COMPAMED 2016

COMPAMED has become the leading international marketplace for suppliers of medical manufacturing. The trade fair, which takes place every November and is co-located to MEDICA in Dusseldorf, has been steadily growing over the past years and shows that medical technology remains a rapidly growing market.

In 2016, the joint pavilion by the IVAM Microtechnology Network, the Product Market “High-tech for Medical Devices”, will be located in Hall 8a again and will...

Im Focus: Ultra-thin ferroelectric material for next-generation electronics

'Ferroelectric' materials can switch between different states of electrical polarization in response to an external electric field. This flexibility means they show promise for many applications, for example in electronic devices and computer memory. Current ferroelectric materials are highly valued for their thermal and chemical stability and rapid electro-mechanical responses, but creating a material that is scalable down to the tiny sizes needed for technologies like silicon-based semiconductors (Si-based CMOS) has proven challenging.

Now, Hiroshi Funakubo and co-workers at the Tokyo Institute of Technology, in collaboration with researchers across Japan, have conducted experiments to...

All Focus news of the innovation-report >>>



Event News

#IC2S2: When Social Science meets Computer Science - GESIS will host the IC2S2 conference 2017

14.10.2016 | Event News

Agricultural Trade Developments and Potentials in Central Asia and the South Caucasus

14.10.2016 | Event News

World Health Summit – Day Three: A Call to Action

12.10.2016 | Event News

Latest News

Resolving the mystery of preeclampsia

21.10.2016 | Health and Medicine

Stanford researchers create new special-purpose computer that may someday save us billions

21.10.2016 | Information Technology

From ancient fossils to future cars

21.10.2016 | Materials Sciences

More VideoLinks >>>