Ribosome recycling factor

Last updated
Ribosome recycling factor
Identifiers
SymbolRRF
Pfam PF01765
InterPro IPR002661
CATH 1ek8
SCOP2 1ek8 / SCOPe / SUPFAM
CDD cd00520
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
MRRF
Identifiers
Aliases MRRF , MRFF, MTRRF, RRF, mitochondrial ribosome recycling factor
External IDs OMIM: 604602; MGI: 1915121; HomoloGene: 12203; GeneCards: MRRF; OMA:MRRF - orthologs
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 Mb Chr 2: 36.03 – 36.08 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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

Related Research Articles

Bacterial translation is the process by which messenger RNA is translated into proteins in bacteria.

A release factor is a protein that allows for the termination of translation by recognizing the termination codon or stop codon in an mRNA sequence. They are named so because they release new peptides from the ribosome.

<span class="mw-page-title-main">EF-Tu</span> Prokaryotic elongation factor

EF-Tu is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. It is found in eukaryotic mitochondria as TUFM.

Elongation factor 4 (EF-4) is an elongation factor that is thought to back-translocate on the ribosome during the translation of RNA to proteins. It is found near-universally in bacteria and in eukaryotic endosymbiotic organelles including the mitochondria and the plastid. Responsible for proofreading during protein synthesis, EF-4 is a recent addition to the nomenclature of bacterial elongation factors.

<span class="mw-page-title-main">EEF1G</span> Protein-coding gene in the species Homo sapiens

Elongation factor 1-gamma is a protein that in humans is encoded by the EEF1G gene.

<span class="mw-page-title-main">MRPS12</span> Protein-coding gene in the species Homo sapiens

28S ribosomal protein S12, mitochondrial is a protein that in humans is encoded by the MRPS12 gene.

<span class="mw-page-title-main">DDX41</span> Protein-coding gene in the species Homo sapiens

Probable ATP-dependent RNA helicase DDX41 is an enzyme that in humans is encoded by the DDX41 gene.

<span class="mw-page-title-main">EIF5B</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 5B is a protein that in humans is encoded by the EIF5B gene.

<span class="mw-page-title-main">MRPS30</span> Protein-coding gene in the species Homo sapiens

28S ribosomal protein S30, mitochondrial is a protein that in humans is encoded by the MRPS30 gene.

<span class="mw-page-title-main">MRPS7</span> Protein-coding gene in the species Homo sapiens

28S ribosomal protein S7, mitochondrial is a protein that in humans is encoded by the MRPS7 gene.

<span class="mw-page-title-main">Mitochondrial ribosomal protein L12</span> Protein-coding gene in the species Homo sapiens

39S ribosomal protein L12, mitochondrial is a protein that in humans is encoded by the MRPL12 gene.

<span class="mw-page-title-main">GFM1</span> Protein-coding gene in the species Homo sapiens

Elongation factor G 1, mitochondrial is a protein that in humans is encoded by the GFM1 gene. It is an EF-G homolog.

<span class="mw-page-title-main">MRPS28</span> Protein-coding gene in the species Homo sapiens

28S ribosomal protein S28, mitochondrial is a protein that in humans is encoded by the MRPS28 gene.

<span class="mw-page-title-main">MRPS24</span> Protein-coding gene in the species Homo sapiens

28S ribosomal protein S24, mitochondrial is a protein that in humans is encoded by the MRPS24 gene.

<span class="mw-page-title-main">MRPS17</span> Protein-coding gene in the species Homo sapiens

28S ribosomal protein S17, mitochondrial is a protein that in humans is encoded by the MRPS17 gene.

<span class="mw-page-title-main">EF-G</span> Prokaryotic elongation factor

EF-G is a prokaryotic elongation factor involved in mRNA translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.

<span class="mw-page-title-main">Mitochondrial ribosomal protein L17</span> Protein-coding gene in the species Homo sapiens

39S ribosomal protein L17, mitochondrial is a protein that in humans is encoded by the MRPL17 gene.

<span class="mw-page-title-main">Mitochondrial ribosomal protein L10</span> Protein-coding gene in the species Homo sapiens

39S ribosomal protein L10, mitochondrial is a protein that in humans is encoded by the MRPL10 gene.

<span class="mw-page-title-main">Mitochondrial translational release factor 1</span> Protein-coding gene in the species Homo sapiens

Mitochondrial translational release factor 1, also known as MTRF1 is a human gene.

<span class="mw-page-title-main">GFM2</span> Protein-coding gene in the species Homo sapiens

Ribosome-releasing factor 2, mitochondrial is a protein that in humans is encoded by the GFM2 gene. Unlike the other EF-G homolog GFM1, GFM2 functions as a Ribosome Recycling Factor in termination.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000148187 – Ensembl, May 2017
  2. 1 2 3 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.
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