The psychrotropic bacterium, Pseudoalteromonas sp. QI-1, which produces extracellular cold-active protease, was
isolated from Antarctic seawater. The genomic DNA of this bacterium was used to construct a plasmid genomic library with the
goal of screening cold-active protease genes. Gene pro-2127 with an open reading frame of 2127 bp encoding protease
PRO-2127 was cloned and sequenced. Alignment of amino acid sequences suggested that the precursor of PRO-2127 was a
member of subfamily S8A, and that it might contain four domains: a signal peptide, an N-terminal prosequence, a catalytic
domain and a C-terminal extension. Amino acids Asp185, His244 and Ser425 might form a catalytic triad. PRO-2127 showed
some structural features common to psychrophilic enzymes, such as a decrease in Arg residues and the Arg/(Arg+Lys) ratio.
Heterologous expression of pro-2127 in
RESEARCH-ARTICLE
Cloning and heterologous expression of pro-2127, a gene encoding cold-active protease from sp. QI-1

Vol. 22, Issue 2, pp. 124-130 (2011) • DOI
Abstract
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Abstract
Author Address:
1. Key Lab of Marine Bioactive Substances, SOA, Qingdao 266061, China;
2. First Institute of Oceanography, SOA, Qingdao 266061, China
2. First Institute of Oceanography, SOA, Qingdao 266061, China
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