Zuotin
Identifiers
OrganismSaccharomyces cerevisiae
SymbolZUO1
UniProtP32527
Search for
StructuresSwiss-model
DomainsInterPro

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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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.
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