ZUO1/YGR285C Summary Help

Standard Name ZUO1 1
Systematic Name YGR285C
Feature Type ORF, Verified
Description Ribosome-associated chaperone; functions in ribosome biogenesis and, in partnership with Ssz1p and SSb1/2, as a chaperone for nascent polypeptide chains; contains a DnaJ domain and functions as a J-protein partner for Ssb1p and Ssb2p (2, 3, 4, 5 and see Summary Paragraph)
Gene Product Alias zuotin 1
Chromosomal Location
ChrVII:1063153 to 1061852 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ZUO1 GO evidence and references
  View Computational GO annotations for ZUO1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Classical genetics
Large-scale survey
139 total interaction(s) for 102 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 57
  • Affinity Capture-RNA: 6
  • Affinity Capture-Western: 12
  • Biochemical Activity: 2
  • Co-crystal Structure: 1
  • Co-fractionation: 1
  • PCA: 1
  • Reconstituted Complex: 2
  • Two-hybrid: 3

Genetic Interactions
  • Dosage Rescue: 5
  • Negative Genetic: 9
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 2
  • Positive Genetic: 13
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 5
  • Synthetic Rescue: 10

Expression Summary
Length (a.a.) 433
Molecular Weight (Da) 49,019
Isoelectric Point (pI) 8.8
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:1063153 to 1061852 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1302 1063153..1061852 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003517

Hsp40/DnaJ is a family of proteins, established by bacterial DnaJ, that regulates Hsp70 chaperone activity. Hsp40s stimulate the intrinsically weak ATPase activity of Hsp70 proteins and facilitate Hsp70 interaction with polypeptide substrates. Hsp70 family members often have multiple Hsp40 partners, and these specific pairings govern Hsp70 chaperone involvement in particular processes (reviewed in 6, 7, and 8). All Hsp40s contain a highly conserved 75-amino acid J domain, which interacts with the ATPase domain of Hsp70 to stimulate ATP hydrolysis. However, there are also other conserved structural domains, and based on the presence or absence of these regions, the Hsp40 family can be divided into three subtypes: type I, type II and type III (a comprehensive overview of the structural features of the different HSP40 subtypes can be found in 8). Sequence analysis of the S. cerevisiae genome has revealed 22 proteins in the Hsp40/DnaJ family: YDJ1, XDJ1, APJ1, SIS1, DJP1, ZUO1, SWA2, JJJ1, JJJ2, JJJ3, CAJ1, CWC23, MDJ1, MDJ2, PAM18, JAC1, JID1, SCJ1, HLJ1, JEM1, SEC63, and ERJ5 (8).

ZUO1 encodes zuotin, a ribosome-associated DnaJ-like protein that may act in conjunction with the Hsp70 proteins Ssb1p and Ssb2p to chaperone the folding of nascent polypeptide chains (2). Zuo1p was first identified as a Z-DNA binding protein (1), and was also found to bind tRNAs (9). Given its nucleic acid binding characteristics, Zuo1p likely associates with ribosomes via an interaction with the rRNA (2). Cells lacking Zuo1p show slow growth and sensitivity to low temperatures, high osmolarity, and certain protein synthesis inhibitors (2, 1).

Last updated: 2000-05-01 Contact SGD

References cited on this page View Complete Literature Guide for ZUO1
1) Zhang S, et al.  (1992) Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae. EMBO J 11(10):3787-96
2) Yan W, et al.  (1998) Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J 17(16):4809-17
3) Gautschi M, et al.  (2001) RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc Natl Acad Sci U S A 98(7):3762-7
4) Huang P, et al.  (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12(6):497-504
5) Albanese V, et al.  (2010) A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J Cell Biol 189(1):69-81
6) Qiu XB, et al.  (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560-2570
7) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
8) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71
9) Wilhelm ML, et al.  (1994) Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae. FEBS Lett 349(2):260-4