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Zuotin

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.

In 1990, Shuguang Zhang of MIT made a serendipitous discovery of a self-assembling peptide in yeast protein Zuotin.[3][4] 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.[5][6][7][8]

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.[9][10]

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.

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