Molecular chaperones (see figure) are type of proteins that assist fixing of denatured proteins by helping them to refold smoothly. Heat shock protein (Hsp) is one type of such chaperones and they are found universally among living species; from plants; to bacteria; to animals. Recent studies revealed that Hsp also play crucial roles besides defense mechanism against physical damage. They serve as a “genetic buffer” to minimize the effect of random genetic variations by covering these changes; a phenomenon known as “canalization”, which was first coined by Waddington in 1940.
Studies on various model species such as Drosophila melanogaster and Alabidopsis thaliana have proven that inhibition of Hsp90 causes sudden appearance of previously masked phenotypes. This result suggests that Hsp90 is protecting genes from harmful mutations as well as maintaining the potential for evolution, or “evolvability” by accumulating, rather than discarding these variations. Korcsmaros et al. (2007) explains this complex function of Hsp family is made possible by very weak inter-modular links in chaperones. Further, they discuss a possible application for this multi-function of chaperone family to clinical aspects so called “chaperone therapies”. Examples include non-toxic cancer therapy, anti-aging and treatment for general diseases.
Further research on how chaperones act in cellular level will provide important information for understanding the evolutionary biology and also has numbers of potential applications for clinical uses.
Reference
Flatt T., “The Evolutionary Genetics of Canalization” The Quarterly Review of Biology Vol.80 No.3 287-316
Korcsmaros T, Kovacs I.A, Szalay M.S and Csermely P., 2007 “Molecular chaperones: The modular evolution of cellular networks” Journal of Bioscience. Vol.32 441-446
Mitchell-Olds T and Knight C. A., 2002 “Chaperons as Buffering Agents?” Science, Vol 296 2348-2349
Pigliucci M., 2002. “Buffer zone” Nature Vol. 417. (6) 598-599
Stearns S. C., 2002. “Progress on canalization” Proceeding of Natural Academy of Science. Vol.99 (16) 10229-10230
Studies on various model species such as Drosophila melanogaster and Alabidopsis thaliana have proven that inhibition of Hsp90 causes sudden appearance of previously masked phenotypes. This result suggests that Hsp90 is protecting genes from harmful mutations as well as maintaining the potential for evolution, or “evolvability” by accumulating, rather than discarding these variations. Korcsmaros et al. (2007) explains this complex function of Hsp family is made possible by very weak inter-modular links in chaperones. Further, they discuss a possible application for this multi-function of chaperone family to clinical aspects so called “chaperone therapies”. Examples include non-toxic cancer therapy, anti-aging and treatment for general diseases.
Further research on how chaperones act in cellular level will provide important information for understanding the evolutionary biology and also has numbers of potential applications for clinical uses.
Reference
Flatt T., “The Evolutionary Genetics of Canalization” The Quarterly Review of Biology Vol.80 No.3 287-316
Korcsmaros T, Kovacs I.A, Szalay M.S and Csermely P., 2007 “Molecular chaperones: The modular evolution of cellular networks” Journal of Bioscience. Vol.32 441-446
Mitchell-Olds T and Knight C. A., 2002 “Chaperons as Buffering Agents?” Science, Vol 296 2348-2349
Pigliucci M., 2002. “Buffer zone” Nature Vol. 417. (6) 598-599
Stearns S. C., 2002. “Progress on canalization” Proceeding of Natural Academy of Science. Vol.99 (16) 10229-10230
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