Hsp70

Hsp70 is a family of heat shock proteins including HSP70 (also known as Hsp72), Bip and the prokaryotic protein DnaK with an approximate molecular weight of 70 kDa. In most species there are many proteins that belong to the Hsp70 family. All Hsp70 proteins bind ATP. Research suggest that they play an important role in the transport of proteins across membranes, and in protein folding. Their precise mechanism of function is not yet known.

The molecular chaperones Hsp70 and Hsp90 are of crucial importance for the maturation and folding of a diverse set of substrate proteins. Members of the Hsp70 family are strongly upregulated by heat stress and chemical toxins, particularly heavy metals such as arsenic, cadmium, copper, mercury, etc. It was originally discovered by FM Rotissa in the 1960s when a lab worker accidently boosted the incubation temperature of Drosophila (fruit flies). When examing the chrosomes, Rotissa found a "puffing pattern" indicated heightened gene transcription. This was later described at the Heat Shock Response (i.e. Hsp proteins).

See also

• michondrial-import stimulation factor

External links

• http://pfam.wustl.edu/cgi-bin/getdesc?name=HSP70
• Diagram of the domain structure of Hsp70 (Page no longer exists)

References

• Wegele H, Muller L, Buchner J. (2004). Hsp70 and Hsp90 – a relay team for protein folding. Rev Physiol Biochem Pharmacol 151:1–44