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Gene cloning of cold-adapted isocitrate lyase from a psychrophilic bacterium, Colwellia psychrerythraea, and analysis of amino acid residues involved in cold adaptation of this enzyme

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Title: Gene cloning of cold-adapted isocitrate lyase from a psychrophilic bacterium, Colwellia psychrerythraea, and analysis of amino acid residues involved in cold adaptation of this enzyme
Authors: Sato, Yuhya Browse this author
Watanabe, Seiya Browse this author
Yamaoka, Naoto Browse this author
Takada, Yasuhiro Browse this author →KAKEN DB
Keywords: psychrophlic bacterium
Colwellia psychrerythraea
isocitrate lyase
cold-adapted enzyme
cold-inducible gene expression
Issue Date: Jan-2008
Publisher: Springer
Journal Title: Extremophiles
Volume: 12
Issue: 1
Start Page: 107
End Page: 117
Publisher DOI: 10.1007/s00792-007-0115-9
PMID: 17965824
Abstract: The gene (icl) encoding cold-adapted isocitrate lyase (ICL) of a psychrophilic bacterium, Colwellia psychrerythraea, was cloned and sequenced. Open reading frame of the gene was 1,587 bp in length and corresponded to a polypeptide composed of 528 amino acids. The deduced amino acid sequence showed high homology with that of cold-adapted ICL from other psychrophilic bacterium, C. maris (88% identity), but the sequential homology with that of the Escherichia coli ICL was low (28% identity). Primer extension analysis revealed that transcriptional start site for the C. psychrerythraea icl gene was guanine, located at 87 bases upstream of translational initiation codon. The expression of this gene in the cells of an E. coli mutant defective in ICL was induced by not only low temperature but also acetate. However, cis-acting elements for cold-inducible expression known in the several other bacterial genes were absent in the promoter region of the C. psychrerythraea icl gene. The substitution of Ala214 for Ser in the C. psychrerythraea ICL introduced by point mutation resulted in the increased thermostability and lowering of the specific activity at low temperature, indicating that Ala214 is important for psychrophilic properties of this enzyme.
Rights: The original publication is available at www.springerlink.com
Relation: http://www.springerlink.com
Type: article (author version)
URI: http://hdl.handle.net/2115/32824
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 高田 泰弘

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