CNS1 HSP70/90 family co-chaperone CNS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: CNS1
Official Full Name: HSP70/90 family co-chaperone CNS1
Primary source: SGD:S000000359
Locus tag: YBR155W
See related: AllianceGenome:SGD:S000000359; FungiDB:YBR155W; VEuPathDB:YBR155W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables Hsp70 protein binding activity; Hsp90 protein binding activity; and ribosome binding activity. Involved in protein refolding. Located in cytoplasm. Orthologous to human TTC4 (tetratricopeptide repeat domain 4). [provided by Alliance of Genome Resources, Dec 2024]
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Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

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Chaperoning of eEF2 by Cns1 is essential for yeast viability and requires a defined subset of the Hsp90 machinery as well as the identified eEF2 recruiting factor Hgh1.
Title: The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
overexpression of other co-chaperones further disrupts the essential functions of Cns1 and Sgt1. However, the specificity of the negative effects indicates that only a subset of co-chaperones competes with Sgt1 or Cns1 for binding to Hsp90.
Title: Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.
CNS1 binds intact ribosome.
Title: The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome.
Cns1p, a cochaperone for Hsp70 and Hsp90 chaperones, is a strong inhibitor of TBSV replication.
Title: Identification of novel host factors via conserved domain search: Cns1 cochaperone is a novel restriction factor of tombusvirus replication in yeast.
Cns1 is a potent cochaperone of Ssa1
Title: Cns1 is an activator of the Ssa1 ATPase activity.

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables Hsp70 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp70 protein binding	IDA Inferred from Direct Assay more info	PubMed
enables Hsp90 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp90 protein binding	IDA Inferred from Direct Assay more info	PubMed
enables Hsp90 protein binding	IEA Inferred from Electronic Annotation more info
enables ribosome binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IPI Inferred from Physical Interaction more info	PubMed
involved_in protein refolding	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IPI Inferred from Physical Interaction more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

NP_009713.1

TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant

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The following sections contain reference sequences that belong to a specific genome build. Explain