Poly(A)-binding protein: Difference between revisions
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==Rotavirus NSP3== |
==Rotavirus NSP3== |
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[[Image:Rotavirus Translation.svg|thumb|Cellular vs Rotavirus Translation]] |
[[Image:Rotavirus Translation.svg|thumb|Cellular vs Rotavirus Translation]] |
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[[Rotavirus]] [[RNA-binding protein]] [[NSP3(Rotavirus)|NSP3]] interacts with [[Eukaryotic initiation factor|eIF4GI]] and evicts the poly(A) binding protein from [[Eukaryotic initiation factor|eIF4F]]. And NSP3A, by taking the place of PABP on [[Eukaryotic initiation factor|eIF4GI]], is responsible for the shut-off of cellular protein synthesis.<ref name=pmid9755181>{{Cite journal |pmid=9755181 |doi=10.1093/emboj/17.19.5811 |year=1998 |last1=Piron |first1=M |last2=Vende |last3=Cohen |last4=Poncet |title=Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F |volume=17 |issue=19 |pages=5811–21 |journal=The EMBO |
[[Rotavirus]] [[RNA-binding protein]] [[NSP3(Rotavirus)|NSP3]] interacts with [[Eukaryotic initiation factor|eIF4GI]] and evicts the poly(A) binding protein from [[Eukaryotic initiation factor|eIF4F]]. And NSP3A, by taking the place of PABP on [[Eukaryotic initiation factor|eIF4GI]], is responsible for the shut-off of cellular protein synthesis.<ref name=pmid9755181>{{Cite journal |pmid=9755181 |doi=10.1093/emboj/17.19.5811 |year=1998 |last1=Piron |first1=M |last2=Vende |last3=Cohen |last4=Poncet |title=Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F |volume=17 |issue=19 |pages=5811–21 |journal=The EMBO Journal |format=Free full text |first2=P |first3=J |first4=D |pmc=1170909}}</ref> |
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==Genes== |
==Genes== |
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Revision as of 12:29, 13 April 2012
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Poly(A)-binding protein (PAB or PABP)[1] is a RNA-binding protein which binds to the poly(A) tail of mRNA.[2] The poly(A) tail is located on the 3' end of mRNA. The nuclear isoforms selectively binds to around 50 nucleotides and stimulates the activity of Polyadenylate polymerase.
Expression and binding
The expression of mammalian Poly(A)-binding protein is regulated at the translational level by a feed-back mechanism: the mRNA encoding PABP contains in its 5' UTR an A-rich sequence which binds Poly(A)-binding protein. This leads to repression of translation
The cytosolic isoform of eukaryotes Poly(A) binding protein binds to the initiation factor eIF-4G via its C-terminal domain. EIF-4G is bound to eIF-4E, another initiation factor bound to the 5' cap on the 5' end of mRNA. This binding forms the characteristic loop structure of eukaryotic protein synthesis. Poly(A)-binding protein interacting proteins in the cytosol compete for the eIF-4G binding sites. Poly(A)-binding protein has also been shown to interact with a termination factor (eRF3)
Rotavirus NSP3
Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. And NSP3A, by taking the place of PABP on eIF4GI, is responsible for the shut-off of cellular protein synthesis.[3]
Genes
There are several forms.[4] These include:
References
- ^ Kahvejian A, Svitkin YV, Sukarieh R, M'Boutchou MN, Sonenberg N (2005). "Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms". Genes Dev. 19 (1): 104–13. doi:10.1101/gad.1262905. PMC 540229. PMID 15630022.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Poly(A)-Binding+Proteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- ^ Piron, M; Vende, P; Cohen, J; Poncet, D (1998). "Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F" (Free full text). The EMBO Journal. 17 (19): 5811–21. doi:10.1093/emboj/17.19.5811. PMC 1170909. PMID 9755181.
- ^ Katzenellenbogen RA, Vliet-Gregg P, Xu M, Galloway DA (2010). "Cytoplasmic Poly(A) Binding Proteins Regulate Telomerase Activity and Cell Growth in Human Papillomavirus Type 16 E6-Expressing Keratinocytes". J. Virol. 84 (24): 12934–44. doi:10.1128/JVI.01377-10. PMC 3004306. PMID 20943973.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)
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