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CspB of an arctic bacterium, Polaribacter irgensii KOPRI 22228, confers extraordinary freeze-tolerance
Jung, Youn Hong; Lee, Yoo Kyung; Lee, Hong Kum; Lee, Kyunghee; Im, Hana.
Afiliação
  • Jung, Youn Hong; Sejong University. Department of Molecular Biology. Seoul. South Korea
  • Lee, Yoo Kyung; Korea Ocean Research and Development Institute. Division of Life Sciences. Korea Polar Research Institute. Incheon. South Korea
  • Lee, Hong Kum; Korea Ocean Research and Development Institute. Division of Life Sciences. Korea Polar Research Institute. Incheon. South Korea
  • Lee, Kyunghee; Sejong University. Department of Chemistry. Seoul. South Korea
  • Im, Hana; Sejong University. Department of Molecular Biology. Seoul. South Korea
Braz. J. Microbiol. ; 49(1): 97-103, jan.-mar. 2018. ilus, graf
Article em En | VETINDEX | ID: vti-18673
Biblioteca responsável: BR68.1
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.(AU)
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Texto completo: 1 Base de dados: VETINDEX Idioma: En Revista: Braz. J. Microbiol. Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: VETINDEX Idioma: En Revista: Braz. J. Microbiol. Ano de publicação: 2018 Tipo de documento: Article