Zuotin

Zuotin
Identifiers
OrganismSaccharomyces cerevisiae
SymbolZUO1
OrthologsOMA: entry
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. 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.

In 1990, Shuguang Zhang of MIT made a serendipitous discovery of a self-assembling peptide in yeast protein Zuotin. This discovery led to the development of a new field of peptide nanobiotechnology and to designs of a variety of self-assembling peptides for widespread uses, including peptide hydrogels in materials science, 3D tissue cell culture and tissue engineering, nanomedicine, sustained molecular releases, clinical and surgical applications.

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.

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. ↑ Zhang, Shuguang (October 20, 2017). "Discovery and design of self-assembling peptides". Interface Focus. 7 (6) 20170028. doi:10.1098/rsfs.2017.0028. PMC 5665798. PMID 29147558.
  4. ↑ Zhang, Shuguang (October 11, 1992). "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae". The EMBO Journal. 11 (10): 3787–3796. doi:10.1002/j.1460-2075.1992.tb05464.x. PMC 556839. PMID 1396572.
  5. ↑ "John Simon Guggenheim Foundation - Shuguang Zhang".
  6. ↑ Levin, Aviad (September 15, 2020). "Biomimetic peptide self-assembly for functional materials". Nature Reviews Chemistry. 4 (11): 615–634. doi:10.1038/s41570-020-0215-y. PMC 7617017. PMID 39650726. S2CID 221718855.
  7. ↑ Gelain, Fabrizio (February 17, 2021). "Self-assembling peptide scaffolds in the clinic". npj Regenerative Medicine. 6 (1): 9. doi:10.1038/s41536-020-00116-w. PMC 7889856. PMID 33597509.
  8. ↑ Yang, Jia (2021). "Self-Assembled Peptide Drug Delivery Systems". ACS Appl. Bio Mater. 4 (1): 24–46. doi:10.1021/acsabm.0c00707. PMID 35014275. S2CID 225639201.
  9. ↑ 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.
  10. ↑ 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.