Heat Shock Proteins in the Terrestrial Epilithic Cyanobacterium Tolypothrix byssoidea

Abstract

The cyanobacterial crust occurring in desiccated state exposed to high temperature and solar radiation on the rock surface contained several low molecular mass (LMM) proteins (10.5, 13, and 25 kDa), water stress protein (wsp, 39 kDa), additional proteins (43 and 49 kDa), a chaperonin (58 kDa), and a stress-induced protein (84 kDa). When the crust was exposed to UV-C radiation, it counteracted the UV-B damage by overproduction of certain proteins and synthesis of two high molecular mass (HMM) proteins. Exposure of the crust to heat had an adverse effect on the survival of the organism there-in which was due to repression of few proteins. Unlike the modification pattern of protein synthesis in the cyanobacterium inhabiting the crust, the same organism grown in culture could tolerate heat by synthesizing two HMM proteins. Several proteins of diverse groups were repressed in the cyanobacterium in culture upon exposure to UV-C, which was counteracted by induction of three new polypeptides (chaperonin and HMMs), and overproduction of one 41 kDa protein.