TAILIEUCHUNG - Báo cáo Y học: Functional analysis of a small heat shock/a-crystallin protein from Artemia franciscana

Oviparously developing embryos of the brine shrimp, Artemia franciscana, synthesize abundant quantities of a small heat shock/a-crystallin protein, termed p26. Wild-type p26 functions as a molecular chaperone in vitro and is thought to help encysted Artemia embryos survive severe physiological stress encountered during diapause and anoxia. Full-length and truncated p26 cDNA derivatives were generated by PCR amplification of p26-3-6-3, then cloned in either pET21(+) or pRSETC and expressed in Escherichia coli BL21(DE3) | Eur. J. Biochem. 269 933-942 2002 FEBS 2002 Functional analysis of a small heat shock a-crystallin protein from Artemia franciscana Oligomerization and thermotolerance Julie A. Crack Marc Mansour Yu Sun and Thomas H. MacRae Department of Biology Dalhousie University Halifax Nova Scotia Canada Oviparously developing embryos of the brine shrimp Artemia franciscana synthesize abundant quantities of a small heat shock a-crystallin protein termed p26. Wild-type p26 functions as a molecular chaperone in vitro and is thought to help encysted Artemia embryos survive severe physiological stress encountered during diapause and anoxia. Full-length and truncated p26 cDNA derivatives were generated by PCR amplifcation of p26-3-6-3 then cloned in either pET21 or pRSETC and expressed in Escherichia coli BL21 DE3 . All constructs gave a polypeptide detectable on Western blots with either p26 specific antibody or with antibody to the His6 epitope tag encoded by pRSETC. Full-length p26 in cell-free extracts of E. coli was about equal in mass to that found in Artemia embryos but p26 lacking N- and C-terminal residues remained either as monomers or small multimers. All p26 constructs conferred thermotolerance on transformed E. coli although not all formed oligomers and cells expressing N-terminal truncated derivatives of p26 were more heat resistant than bacteria expressing p26 with C-terminal deletions. The C-terminal extension of p26 is seemingly more important for thermotolerance than is the N-terminus and p26 protects E. coli against heat shock when oligomer size and protein concentration are low. The fndings have important implications for understanding the functional mechanisms of small heat shock a-crystallin proteins. Keywords small heat shock a-crystallin protein oligomerization thermotolerance diapause Artemia franciscana. Cells respond to stress by the enhanced synthesis of heat shock or stress proteins which are also developmentally regulated under normal physiological .

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