Z-DNA binding protein 1, also known as Zuotin, is a Saccharomyces cerevisiae yeast gene.
| Zuotin | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | ZUO1 | ||||||
| UniProt | P32527 | ||||||
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Zuo1 has been identified in vitro as a tRNA and Z-DNA binding protein.[1][2] The name "zuotin" is derived from the Chinese word "zuo" meaning "left". It is a member of Hsp40 family. Like all other Hsp40 members it also contains a classic J domain.
Zuotin and related proteins contain a unique Zuotin homology domain (ZHD). It associates with the Hsp70 family Ssz1 to form a ribosome associated complex (RAC). In such a complex, the N-terminal domains (including the J domain) associates with Ssz1p on the surface of the large (60S) ribosomal subunit. ZHD provides further contacts with the 60S subunit and connects to a subunit-spanning medium domain (MD), the "neck" of RAC. The four-helix-bundle RAC head domain is located at the C-terminus and binds the small (40S) subunit. The J domain-Ssz1p complex, located over the peptide exit tunnel of the large ribosomal subunit, helps the nascent peptide fold.[3][4]
References
edit- ^ Zhang S, Lockshin C, Herbert A, Winter E, Rich A (October 1992). "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae". The EMBO Journal. 11 (10): 3787–96. doi:10.1002/j.1460-2075.1992.tb05464.x. PMC 556839. PMID 1396572.3787-96&rft.date=1992-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC556839#id-name=PMC&rft_id=info:pmid/1396572&rft_id=info:doi/10.1002/j.1460-2075.1992.tb05464.x&rft.aulast=Zhang&rft.aufirst=S&rft.au=Lockshin, C&rft.au=Herbert, A&rft.au=Winter, E&rft.au=Rich, A&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC556839&rfr_id=info:sid/en.wikipedia.org:Zuotin" class="Z3988">
- ^ Wilhelm ML, Reinbolt J, Gangloff J, Dirheimer G, Wilhelm FX (August 1994). "Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae". FEBS Letters. 349 (2): 260–4. doi:10.1016/0014-5793(94)00683-0. PMID 8050578.260-4&rft.date=1994-08&rft_id=info:doi/10.1016/0014-5793(94)00683-0&rft_id=info:pmid/8050578&rft.aulast=Wilhelm&rft.aufirst=ML&rft.au=Reinbolt, J&rft.au=Gangloff, J&rft.au=Dirheimer, G&rft.au=Wilhelm, FX&rft_id=https://doi.org/10.1016%2F0014-5793%2894%2900683-0&rfr_id=info:sid/en.wikipedia.org:Zuotin" class="Z3988">
- ^ Leidig C, Bange G, Kopp J, Amlacher S, Aravind A, Wickles S, et al. (January 2013). "Structural characterization of a eukaryotic chaperone--the ribosome-associated complex". Nature Structural & Molecular Biology. 20 (1): 23–8. doi:10.1038/nsmb.2447. PMID 23202586. S2CID 22950001.23-8&rft.date=2013-01&rft_id=https://api.semanticscholar.org/CorpusID:22950001#id-name=S2CID&rft_id=info:pmid/23202586&rft_id=info:doi/10.1038/nsmb.2447&rft.aulast=Leidig&rft.aufirst=C&rft.au=Bange, G&rft.au=Kopp, J&rft.au=Amlacher, S&rft.au=Aravind, A&rft.au=Wickles, S&rft.au=Witte, G&rft.au=Hurt, E&rft.au=Beckmann, R&rft.au=Sinning, I&rfr_id=info:sid/en.wikipedia.org:Zuotin" class="Z3988">
- ^ Lee K, Sharma R, Shrestha OK, Bingman CA, Craig EA (November 2016). "Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits". Nature Structural & Molecular Biology. 23 (11): 1003–1010. doi:10.1038/nsmb.3299. PMC 5097012. PMID 27669034.1003-1010&rft.date=2016-11&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5097012#id-name=PMC&rft_id=info:pmid/27669034&rft_id=info:doi/10.1038/nsmb.3299&rft.aulast=Lee&rft.aufirst=K&rft.au=Sharma, R&rft.au=Shrestha, OK&rft.au=Bingman, CA&rft.au=Craig, EA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5097012&rfr_id=info:sid/en.wikipedia.org:Zuotin" class="Z3988">