Ribosome recycling factor

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Ribosome recycling factor
Identifiers
SymbolRRF
PfamPF01765
InterProIPR002661
CATH1ek8
SCOP21ek8 / SCOPe / SUPFAM
CDDcd00520
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
MRRF
Identifiers
AliasesMRRF, MRFF, MTRRF, RRF, mitochondrial ribosome recycling factor
External IDsOMIM: 604602 MGI: 1915121 HomoloGene: 12203 GeneCards: MRRF
Orthologs
SpeciesHumanMouse
Entrez

92399

67871

Ensembl

ENSG00000148187

ENSMUSG00000026887

UniProt

Q96E11

Q9D6S7

RefSeq (mRNA)

NM_026422

RefSeq (protein)

NP_080698

Location (UCSC)Chr 9: 122.26 – 122.33 MbChr 2: 36.03 – 36.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ribosome recycling factor or ribosome release 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 (bacterial translation). In humans, the mitochrondrial version is coded by the MRRF gene.

Discovery

The ribosome recycling factor was discovered in the early 1970s by the work of Akira Kaji and Akikazu Hiroshima at the University of Pennsylvania.[5][6][7][8] 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.

Function

RRF accomplishes the recycling of ribosomes by splitting ribosomes into subunits, thereby releasing the bound mRNA. This also requires the participation of EF-G (GFM2 in humans).[9] Depending on the tRNA, IF1–IF3 may also perform recycling.[10]

Loss of RRF function

Structure and binding to ribosomes

The crystal structure of RRF was first determined by X-ray diffraction in 1999.[13] 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.[14] 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.

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000148187 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026887 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hirashima A, Kaji A (November 1970). "Factor dependent breakdown of polysomes". Biochem. Biophys. Res. Commun. 41 (4): 877–883. doi:10.1016/0006-291X(70)90165-8. PMID 4920474.
  6. ^ Hirashima A, Kaji A (March 1972). "Factor-dependent release of ribosomes from messenger RNA. Requirement for two heat-stable factors". J. Mol. Biol. 65 (1): 43–58. doi:10.1016/0022-2836(72)90490-1. PMID 4553259.
  7. ^ Hirashima A, Kaji A (October 1972). "Purification and properties of ribosome-releasing factor". Biochemistry. 11 (22): 4037–4044. doi:10.1021/bi00772a005. PMID 4563926.
  8. ^ Hirashima A, Kaji A (November 1973). "Role of elongation factor G and a protein factor on the release of ribosomes from messenger ribonucleic acid". J. Biol. Chem. 248 (21): 7580–7587. doi:10.1016/S0021-9258(19)43330-9. PMID 4583357.
  9. ^ Hirokawa G, Demeshkina N, Iwakura N, Kaji H, Kaji A (March 2006). "The ribosome-recycling step: Consensus or controversy?". Trends Biochem. Sci. 31 (3): 143–149. doi:10.1016/j.tibs.2006.01.007. PMID 16487710.
  10. ^ Pavlov, MY; Antoun, A; Lovmar, M; Ehrenberg, M (18 June 2008). "Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting". The EMBO Journal. 27 (12): 1706–17. doi:10.1038/emboj.2008.99. PMC 2435134. PMID 18497739.
  11. ^ Janosi L, Shimizu I, Kaji A (May 1994). "Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth". Proc. Natl. Acad. Sci. U.S.A. 91 (10): 4249–4253. Bibcode:1994PNAS...91.4249J. doi:10.1073/pnas.91.10.4249. PMC 43762. PMID 8183897.
  12. ^ Teyssier E, Hirokawa G, Tretiakova A, Jameson B, Kaji A, Kaji H (July 2003). "Temperature-sensitive mutation in yeast mitochondrial ribosome recycling factor (RRF)". Nucleic Acids Res. 31 (14): 4218–4226. doi:10.1093/nar/gkg449. PMC 165964. PMID 12853640.
  13. ^ Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A (December 1999). "Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic". Science. 286 (5448): 2349–2352. doi:10.1126/science.286.5448.2349. PMID 10600747.
  14. ^ Agrawal RK, Sharma MR, Kiel MC, et al. (June 2004). "Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications". Proc. Natl. Acad. Sci. U.S.A. 101 (24): 8900–8905. Bibcode:2004PNAS..101.8900A. doi:10.1073/pnas.0401904101. PMC 428444. PMID 15178758.

External links

Retrieved from "https://mdwiki.org/wiki/Ribosome_recycling_factor"