AHA1/YDR214W Summary Help

AHA1 BASIC INFORMATION

Standard Name AHA1 1
Systematic Name YDR214W
Feature Type ORF, Verified
Description Co-chaperone that binds to Hsp82p and activates its ATPase activity; similar to Hch1p; expression is regulated by stresses such as heat shock (1, 2 and see Summary Paragraph)
Name Description Activator of Heat shock protein 90 ATPase 1
GO Annotations All AHA1 GO evidence and references
    View Computational GO annotations for AHA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All AHA1 Phenotype details and references
Large-scale survey
null
Interactions AHA1 All interactions details and references
65 total interaction(s) for 43 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 46
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 2
  • Co-crystal Structure: 1
  • Reconstituted Complex: 2
  • Two-hybrid: 11

Genetic Interactions
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1

Sequence Information
ChrIV:892873 to 893925 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2008-06-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1053 892873..893925 2008-06-05 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002622

AHA1 RESOURCES

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Expression Summary histogram

SUMMARY PARAGRAPH for AHA1

AHA1 and the closely related gene HCH1 encode cochaperones that regulate the activity of members of the HSP90 family (Hsp82p and Hsc82p in S. cerevisiae; 1, 3). The presence of Aha1p and Hch1p, although not required for ATP hydrolysis, is able to stimulate the ATPase activity of Hsp82p/Hsc82p five- to twelve-fold (1, 3). The N-terminal domain of Aha1p, which is equivalent to the entirety of Hch1p, binds to the middle domain of Hsp82p/Hsc82p and promotes a conformational change in the chaperone proteins that enhances their ability to bind ATP (3, 4, 2).

Expression of AHA1 is induced by stress, a process mediated by the transcriptional activator Hsf1p which binds to three heat shock elements in the AHA1 promoter (1). AHA1 is not required for growth under optimal conditions but is essential for survival in cells under stress (1, 3).

Aha1p is a highly conserved protein with similar proteins identified in S. pombe, worms, plants, flies, mice, and humans (3).

Last updated: 2006-06-30

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for AHA1]

1) Panaretou B, et al.  (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10(6):1307-18
2) Siligardi G, et al.  (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem 279(50):51989-98
3) Lotz GP, et al.  (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35
4) Meyer P, et al.  (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23(6):1402-10