![]() irgensii CspB bound to oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. The most common mechanism of Csp function in cold adaption is melting of the secondary structures in RNA and DNA molecules, thus facilitating transcription and translation at low temperatures. Sequence analysis showed that this protein consists of a unique domain at its N-terminal end and a well conserved cold shock domain at its C-terminal end. coli csp-quadruple deletion strain, BX04. It also suppressed the cold-sensitivity of an E. A gene coding for a Csp-family protein, cspB, was cloned from an arctic bacterium, Polaribacter irgensii KOPRI 22228, and overexpression of cspB greatly increased the freeze-survival rates of Escherichia coli hosts, to a greater level than any previously reported Csp. Among the cold-induced proteins, cold shock protein (Csp) family proteins are the most prominent. ![]() Organisms adapted to polar regions possess distinct mechanisms that enable them to survive in extremely cold environments. ![]() Decreased membrane fluidity, uninvited secondary structure formation in nucleic acids, and protein cold-denaturation all occur at cold temperatures. Freezing temperatures are a major challenge for life at the poles. ![]()
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