Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional analysis of a conserved amino-terminal region of HSP70 by site-directed mutagenesis.

Yeast (Chichester, England) - 1 Oct 1991

Nicolet C M, Craig E A

Abstract excerpt

Hsp70 proteins have been highly conserved throughout evolution. As a first step in a structure-function analysis of hsp70, we constructed and analysed the consequences of mutations in a portion of the SSA1 gene, a member of the Saccharomyces cerevisiae HSP70 multigene family, that encodes a nearly invariant region near the amino terminus. Analysis of strains expressing SSA1 proteins with alterations at positions...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Sequence
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genes, Fungal

Share to Genetic Complementation Test

Share to Molecular Sequence Data

Share to Phenotype

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 1776361
DOI: 10.1002/yea.320070706

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of a conserved amino-terminal region of HSP70 by site-directed mutagenesis.PMID 1776361Read ↗

Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Semantic proximity Read ↗

The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.Semantic proximity Read ↗

Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum.Semantic proximity Read ↗

Redox regulation of yeast Hsp70 modulates protein quality control while directly triggering an Hsf1-dependent cytoprotective responseSemantic proximity Read ↗

Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Semantic proximity Read ↗

Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Semantic proximity Read ↗

The complex evolutionary dynamics of Hsp70s: a genomic and functional perspective.Semantic proximity Read ↗

In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae.Semantic proximity Read ↗

Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation.Semantic proximity Read ↗

Sti1 is a novel activator of the Ssa proteins.Semantic proximity Read ↗

Growth-regulated Hsp70 phosphorylation regulates stress responses and prion maintenanceSemantic proximity Read ↗

Suppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.