Ribosome Recycling Factor: Difference between revisions
Jump to navigation
Jump to search
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +)) |
m (refs using AWB) |
||
| Line 1: | Line 1: | ||
{{protein | {{infobox protein | ||
| Name = mitochondrial ribosome recycling factor | | Name = mitochondrial ribosome recycling factor | ||
| caption = | | caption = | ||
| Line 21: | Line 21: | ||
== Discovery == | == 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]].<ref>{{cite journal |vauthors=Hirashima A, Kaji A |title=Factor dependent breakdown of polysomes |journal=Biochem. Biophys. Res. Commun. |volume=41 |issue=4 |pages=877–83 |date=November 1970 |pmid=4920474 |url=http://linkinghub.elsevier.com/retrieve/pii/0006-291X(70)90165-8 |doi=10.1016/0006-291X(70)90165-8}}</ref><ref>{{cite journal |vauthors=Hirashima A, Kaji A |title=Factor-dependent release of ribosomes from messenger RNA. Requirement for two heat-stable factors |journal=J. Mol. Biol. |volume=65 |issue=1 |pages=43–58 |date=March 1972 |pmid=4553259 |url=http://linkinghub.elsevier.com/retrieve/pii/0022-2836(72)90490-1 |doi=10.1016/0022-2836(72)90490-1}}</ref><ref>{{cite journal |vauthors=Hirashima A, Kaji A |title=Purification and properties of ribosome-releasing factor |journal=Biochemistry |volume=11 |issue=22 |pages=4037–44 |date=October 1972 |pmid=4563926 |doi=10.1021/bi00772a005 }}</ref><ref>{{cite journal |vauthors=Hirashima A, Kaji A |title=Role of elongation factor G and a protein factor on the release of ribosomes from messenger ribonucleic acid |journal=J. Biol. Chem. |volume=248 |issue=21 |pages=7580–7 |date=November 1973 |pmid=4583357 |url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=4583357}}</ref> 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 == | == Function == | ||
Recent evidence suggests RRF may accomplish the recycling of ribosomes by splitting ribosomes into subunits, thereby releasing the bound [[mRNA]]<ref>Hirokawa | Recent evidence suggests RRF may accomplish the recycling of ribosomes by splitting ribosomes into subunits, thereby releasing the bound [[mRNA]].<ref>{{cite journal |vauthors=Hirokawa G, Demeshkina N, Iwakura N, Kaji H, Kaji A |title=The ribosome-recycling step: Consensus or controversy? |journal=Trends Biochem. Sci. |volume=31 |issue=3 |pages=143–9 |date=March 2006 |pmid=16487710 |doi=10.1016/j.tibs.2006.01.007 |url=http://linkinghub.elsevier.com/retrieve/pii/S0968-0004(06)00033-8}}</ref> | ||
===Loss of RRF function=== | |||
*In [[Bacteria]] (specifically [[Escherichia coli]]), loss of the [[gene]] encoding RRF is deleterious <ref>Janosi | *In [[Bacteria]] (specifically ''[[Escherichia coli]]''), loss of the [[gene]] encoding RRF is deleterious.<ref>{{cite journal |vauthors=Janosi L, Shimizu I, Kaji A |title=Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue=10 |pages=4249–53 |date=May 1994 |pmid=8183897 |pmc=43762 |url=http://www.pnas.org/cgi/pmidlookup?view=long&pmid=8183897 |doi=10.1073/pnas.91.10.4249}}</ref> This makes RRF a possible target for new [[antibacterial]] drugs. | ||
*[[Yeast]] [[mitochondrial]] RRF (mtRRF) is encoded by a gene in the [[cell nucleus]]. Loss of function of this [[gene]] leads to mitochondrial [[genome]] instability and [[respiratory]] incompetence <ref>Teyssier | *[[Yeast]] [[mitochondrial]] RRF (mtRRF) is encoded by a gene in the [[cell nucleus]]. Loss of function of this [[gene]] leads to mitochondrial [[genome]] instability and [[respiratory]] incompetence.<ref>{{cite journal |vauthors=Teyssier E, Hirokawa G, Tretiakova A, Jameson B, Kaji A, Kaji H |title=Temperature-sensitive mutation in yeast mitochondrial ribosome recycling factor (RRF) |journal=Nucleic Acids Res. |volume=31 |issue=14 |pages=4218–26 |date=July 2003 |pmid=12853640 |pmc=165964 |url=http://nar.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=12853640 |doi=10.1093/nar/gkg449}}</ref> | ||
== Structure of RRF and Binding to Ribosomes == | == Structure of RRF and Binding to Ribosomes == | ||
The crystal structure of RRF was first determined by [[X-ray diffraction]] in 1999 <ref>Selmer | The crystal structure of RRF was first determined by [[X-ray diffraction]] in 1999.<ref>{{cite journal |vauthors=Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A |title=Crystal structure of ''Thermotoga maritima'' ribosome recycling factor: a tRNA mimic |journal=Science |volume=286 |issue=5448 |pages=2349–52 |date=December 1999 |pmid=10600747 |url=http://www.sciencemag.org/cgi/pmidlookup?view=long&pmid=10600747 |doi=10.1126/science.286.5448.2349}}</ref> 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 [http://www.pharm.kyoto-u.ac.jp/structbl/gallery/structure/rrf.jpg here]. | ||
Despite the tRNA-mimicry, RRF binds to [[ribosomes]] quite differently from the way [[tRNA]] does <ref>Agrawal | Despite the tRNA-mimicry, RRF binds to [[ribosomes]] quite differently from the way [[tRNA]] does.<ref>{{cite journal |vauthors=Agrawal RK, Sharma MR, Kiel MC, etal |title=Visualization of ribosome-recycling factor on the ''Escherichia coli'' 70S ribosome: functional implications |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue=24 |pages=8900–5 |date=June 2004 |pmid=15178758 |pmc=428444 |doi=10.1073/pnas.0401904101 |url=http://www.pnas.org/cgi/pmidlookup?view=long&pmid=15178758}}</ref> 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 == | == See also == | ||
| Line 42: | Line 39: | ||
*[[Prokaryotic translation]] | *[[Prokaryotic translation]] | ||
*[[Ribosome]] | *[[Ribosome]] | ||
== References == | |||
{{reflist}} | |||
==External links== | ==External links== | ||
Revision as of 16:42, 5 June 2016
| mitochondrial ribosome recycling factor | |
|---|---|
| Identifiers | |
| Symbol | MRRF |
| Entrez | 92399 |
| HUGO | 7234 |
| OMIM | 604602 |
| RefSeq | NM_138777 |
| UniProt | Q96E11 |
| Other data | |
| Locus | Chr. 9 q32-q34.1 |
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.
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.[1][2][3][4] 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
Recent evidence suggests RRF may accomplish the recycling of ribosomes by splitting ribosomes into subunits, thereby releasing the bound mRNA.[5]
Loss of RRF function
- In Bacteria (specifically Escherichia coli), loss of the gene encoding RRF is deleterious.[6] This makes RRF a possible target for new antibacterial drugs.
- Yeast mitochondrial RRF (mtRRF) is encoded by a gene in the cell nucleus. Loss of function of this gene leads to mitochondrial genome instability and respiratory incompetence.[7]
Structure of RRF and Binding to Ribosomes
The crystal structure of RRF was first determined by X-ray diffraction in 1999.[8] 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.[9] 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
- ↑ Hirashima A, Kaji A (November 1970). "Factor dependent breakdown of polysomes". Biochem. Biophys. Res. Commun. 41 (4): 877–83. doi:10.1016/0006-291X(70)90165-8. PMID 4920474.
- ↑ 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.
- ↑ Hirashima A, Kaji A (October 1972). "Purification and properties of ribosome-releasing factor". Biochemistry. 11 (22): 4037–44. doi:10.1021/bi00772a005. PMID 4563926.
- ↑ 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): 7580–7. PMID 4583357.
- ↑ Hirokawa G, Demeshkina N, Iwakura N, Kaji H, Kaji A (March 2006). "The ribosome-recycling step: Consensus or controversy?". Trends Biochem. Sci. 31 (3): 143–9. doi:10.1016/j.tibs.2006.01.007. PMID 16487710.
- ↑ 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): 4249–53. doi:10.1073/pnas.91.10.4249. PMC 43762. PMID 8183897.
- ↑ 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): 4218–26. doi:10.1093/nar/gkg449. PMC 165964. PMID 12853640.
- ↑ 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): 2349–52. doi:10.1126/science.286.5448.2349. PMID 10600747.
- ↑ 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): 8900–5. doi:10.1073/pnas.0401904101. PMC 428444. PMID 15178758.
External links
- ribosome+releasing+factor at the US National Library of Medicine Medical Subject Headings (MeSH)