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Systematic name YBR101C
Gene name FES1
Feature type ORF, Verified
Coordinates Chr II:444693..443821
Primary SGDID S000000305

Description of YBR101C: Hsp70 (Ssa1p) nucleotide exchange factor; cytosolic homolog of Sil1p, which is the nucleotide exchange factor for BiP (Kar2p) in the endoplasmic reticulum; protein abundance increases in response to DNA replication stress[1][2]


Community Commentary

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Alleles, Strains, and Phenotypes

Complete Deletion

Allele: deltafes1

Strain Background: W303 (see detailed notes from Rodney Rothstein and Stephan Bartsch for the W303 strain used in the study), RSY801
Phenotype(s): Temperature(Heat) Sensitive

The deletion of the FES1 gene leads to a strong thermosensitive phenotype as well as cycloheximide sensitivity [1] [3]



YBR101C is a suppressor of YDJ1

Strain Background: W303 (see detailed notes from Rodney Rothstein and Stephan Bartsch for the W303 strain used in the study)
Mutation type(s): deletion, point mutation (ydj1-151)

The thermosensitivity and cycloheximide sensitivity of the single deltafes1 and ydj1-151 mutants is partly suppressed in the double mutant. [1] [3]


Physical interaction with SSA1
Purified GST-Fes1p interacts with the ADP-bound form of (His6)-Ssa1p in GST pull down assays [1] [3]

Protein Details

Protein Function/Process

Fes1p is a nucleotide exchange factor that binds to the Hsp70 chaperone Ssa1p and inhibits its ATPase activity. Fes1p does not play an obvious role in protein folding, transport or degradation, but is involved in protein translation (presumably at the initiation step) [1] [3]

Protein Localization

Fes1p is a cytosolic protein (as shown by immunofluorescence and cell fractionation assays using a GFP-Fes1p construct) [1] [3]

Techniques and Reagents

Protein Purification

Fes1p was purified as a GST fusion protein from E. coli [1] [3]



See Help:References on how to add references

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Kabani M, et al. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22(13):4677-89 SGD PMID 12052876
  2. Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.LID - 10.1038/ncb2549 [doi] Nat Cell Biol () SGD PMID 22842922
  3. 3.0 3.1 3.2 3.3 3.4 3.5 submitted by Mehdi Kabani on 2003-03-31

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