This invention identifies Hsp90 mutant residues that affect the chronological lifespan of yeast.

Heat shock protein 90 (Hsp90) are a class of chaperone proteins that are up-regulated in response to elevated temperature and other environmental stresses. They act as chaperones to other cellular proteins and facilitate their proper folding and repair, and aid in the refolding of misfolded client proteins.

This invention identifies Hsp90 mutant residues that affect the chronological lifespan of yeast. These mutations in addition to a deletion in the sch9 allele, the yeast homolog to human kinase AKT, can increase yeast lifespan from 45 to 57 days, approximately 20% longer than the wildtype strain. These genetically engineered yeast strains may have the longest chronological lifespan reported to date.

Applications:

• Model to study aging and longevity factors
• Model to screen compounds that affect lifespan
• A long-lived yeast strain could be used to ferment alcohol in a more efficient and cost effective as an alternative fuel source
• Method to extend lifespan of transgenic farm animals

Market:
Anti-aging and alternative fuel industries are worth billions of dollars.

Related Publication:
BT Scroggins et al. An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol Cell. 2007 Jan 12;25(1):151-159. [PubMed abs]

Preclinical

U.S. Provisional Application No. 60/848,346 filed 09 Sep 2006 (HHS Reference No. E-319-2006/0-US-01)

Inventors:
Bradley T. Scroggins (NCI) et al.

Licensees Sought:
Available for non-exclusive licensing.

Collaborative Research Opportunity:
The National Cancer Institute’s Urologic Oncology Branch is seeking statements of capability or interest from parties interested in collaborative research to further develop, evaluate, or commercialize models to study aging and longevity factors. Please contact John D. Hewes, Ph.D. at 301-435-3121 or hewesj@mail.nih.gov for more information.