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Provedor de dados:  BJM
País:  Brazil
Título:  CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance
Autores:  Jung,Youn Hong
Lee,Yoo Kyung
Lee,Hong Kum
Lee,Kyunghee
Im,Hana
Data:  2018-03-01
Ano:  2018
Palavras-chave:  Cold-shock protein (Csp)
Psychrophile
Cold-resistance
Resumo:  ABSTRACT Freezing temperatures are a major challenge for life at the poles. Decreased membrane fluidity, uninvited secondary structure formation in nucleic acids, and protein cold-denaturation all occur at cold temperatures. Organisms adapted to polar regions possess distinct mechanisms that enable them to survive in extremely cold environments. Among the cold-induced proteins, cold shock protein (Csp) family proteins are the most prominent. 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. It also suppressed the cold-sensitivity of an E. coli csp-quadruple deletion strain, BX04. 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. 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. P. irgensii CspB bound to oligo(dT)-cellulose resins, suggesting single-stranded nucleic acid-binding activity. The unprecedented level of freeze-tolerance conferred by P. irgensii CspB suggests a crucial role for this protein in survival in polar environments.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822018000100097
Editor:  Sociedade Brasileira de Microbiologia
Relação:  10.1016/j.bjm.2017.04.006
Formato:  text/html
Fonte:  Brazilian Journal of Microbiology v.49 n.1 2018
Direitos:  info:eu-repo/semantics/openAccess
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