Biology:Zuotin
| Zuotin | |||||||
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| Organism | |||||||
| Symbol | ZUO1 | ||||||
| UniProt | P32527 | ||||||
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Z-DNA binding protein 1, also known as Zuotin, is a Saccharomyces cerevisiae yeast gene.
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
- ↑ "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae". The EMBO Journal 11 (10): 3787–96. October 1992. doi:10.1002/j.1460-2075.1992.tb05464.x. PMID 1396572.
- ↑ "Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae". FEBS Letters 349 (2): 260–4. August 1994. doi:10.1016/0014-5793(94)00683-0. PMID 8050578.
- ↑ "Structural characterization of a eukaryotic chaperone--the ribosome-associated complex". Nature Structural & Molecular Biology 20 (1): 23–8. January 2013. doi:10.1038/nsmb.2447. PMID 23202586.
- ↑ "Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits". Nature Structural & Molecular Biology 23 (11): 1003–1010. November 2016. doi:10.1038/nsmb.3299. PMID 27669034.
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