To use all functions of this page, please activate cookies in your browser.
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
Ribosome Recycling Factor
Ribosome Recycling Factor (RRF) is a protein found in bacterial cells as well as eukaryotic organelles, specifically mitochondria and chloroplasts. It functions to recycle ribosomes after completion of protein synthesis.
Additional recommended knowledge
RRF was disocvered in the early 1970s by the groundbreaking work of Akira Kaji and Akikazu Hiroshima at the University of Pennsylvania. Their work described the requirement for two protein factors to release ribosomes from mRNA. These two factors were identified as RRF, an unknown protein until then, and Elongation Factor G (EF-G), a protein already identified and known to function in protein synthesis. RRF was originally called Ribosome Releasing Factor but is now called Ribosome Recycling Factor.
Recent evidence suggests RRF may accomplish the recycling of ribosomes by splitting ribosomes into subunits, thereby releasing the bound mRNA.
Loss of RRF Function:
Structure of RRF and Binding to Ribosomes
The crystal structure of RRF was first determined by X-ray diffraction in 1999 . The most striking revelation was that RRF is a near-perfect structural mimic of tRNA, in both size and dimensions. One view of RRF can be seen here.
Despite the tRNA-mimicry, RRF binds to ribosomes quite differently from the way tRNA does . It has been suggested that ribosomes bind proteins (or protein domain) of similar shape and size to tRNA, and this, rather than function, explains the observed structural mimicry.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Ribosome_Recycling_Factor". A list of authors is available in Wikipedia.|