{{Infobox nonhuman protein |Symbol=ZUO1 |UniProt=P32527 |Organism=Saccharomyces cerevisiae }} '''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.<ref>{{cite journal | vauthors = Zhang S, Lockshin C, Herbert A, Winter E, Rich A | title = Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae | journal = The EMBO Journal | volume = 11 | issue = 10 | pages = 3787–96 | date = October 1992 | pmid = 1396572 | pmc = 556839 | doi = 10.1002/j.1460-2075.1992.tb05464.x }}</ref><ref>{{cite journal | vauthors = Wilhelm ML, Reinbolt J, Gangloff J, Dirheimer G, Wilhelm FX | title = Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae | journal = FEBS Letters | volume = 349 | issue = 2 | pages = 260–4 | date = August 1994 | pmid = 8050578 | doi = 10.1016/0014-5793(94)00683-0 | doi-access = free }}</ref> 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.<ref>{{Cite journal|last=Zhang|first=Shuguang|date=October 20, 2017|title=Discovery and design of self-assembling peptides|journal= Interface Focus|volume=7|issue=6|article-number=20170028|doi=10.1098/rsfs.2017.0028|pmid=29147558|pmc=5665798}}</ref><ref>{{Cite journal|last=Zhang|first=Shuguang|date=October 11, 1992|title=Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae.|journal=The EMBO Journal|volume=11|issue=10|pages=3787–3796|doi=10.1002/j.1460-2075.1992.tb05464.x|pmid=1396572|pmc=556839}}</ref> 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.<ref>{{cite web |title=John Simon Guggenheim Foundation - Shuguang Zhang |url=https://www.gf.org/fellows/all-fellows/shuguang-zhang/}}</ref><ref>{{Cite journal|last=Levin|first=Aviad|date=September 15, 2020|title=Biomimetic peptide self-assembly for functional materials.|journal=Nature Reviews Chemistry|volume=4|issue=11|pages=615–634|doi=10.1038/s41570-020-0215-y|pmid=39650726 |s2cid=221718855|pmc=7617017}}</ref><ref>{{Cite journal|last=Gelain|first=Fabrizio|date=February 17, 2021|title=Self-assembling peptide scaffolds in the clinic|journal=npj Regenerative Medicine|volume=6|issue=1|page=9|doi=10.1038/s41536-020-00116-w|pmid=33597509|pmc=7889856}}</ref><ref>{{Cite journal|last=Yang|first=Jia|title=Self-Assembled Peptide Drug Delivery Systems|url=https://pubs.acs.org/doi/10.1021/acsabm.0c00707|journal=ACS Appl. Bio Mater.|year=2021|volume=4|issue=1 |pages=24–46|doi=10.1021/acsabm.0c00707|pmid=35014275 |s2cid=225639201|url-access=subscription}}</ref>
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.<ref>{{cite journal | vauthors = Leidig C, Bange G, Kopp J, Amlacher S, Aravind A, Wickles S, Witte G, Hurt E, Beckmann R, Sinning I | display-authors = 6 | title = Structural characterization of a eukaryotic chaperone--the ribosome-associated complex | journal = Nature Structural & Molecular Biology | volume = 20 | issue = 1 | pages = 23–8 | date = January 2013 | pmid = 23202586 | doi = 10.1038/nsmb.2447 | s2cid = 22950001 }}</ref><ref>{{cite journal | vauthors = Lee K, Sharma R, Shrestha OK, Bingman CA, Craig EA | title = Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits | journal = Nature Structural & Molecular Biology | volume = 23 | issue = 11 | pages = 1003–1010 | date = November 2016 | pmid = 27669034 | pmc = 5097012 | doi = 10.1038/nsmb.3299 }}</ref>
== References == {{Reflist}}
Category:Saccharomyces cerevisiae genes Category:DNA-binding proteins