Identification of a member of the serralysin family isolated from a psychrotrophic bacterium, Pseudomonas fluorescens 114.
An extracellular metalloprotease named No. 114 protease is one of the major secretions of a psychrotrophic bacterium, Pseudomonas fluorescens 114, the cold-adaptation mechanism of which has not been identified. In this study, we purified and cloned No. 114 protease, which is a single polypeptide having a molecular mass of 47 kDa. This protease contains a zinc-binding motif (HEXXHXUGUXH: X, arbitrary amino acid; U, bulky hydrophobic amino acid), glycine-rich repeats (GGXGXD) and no cysteine residue, which are the features specifically found in serralysin subfamily. No. 114 protease has its maximum activity at the temperature of 35-40 degrees C, which is about 20 degrees C lower than that of a serralysin from a mesophilic bacterium, Pseudomonas aeruginosa. All these results imply that No. 114 protease from this psychrophilic bacterium is a unique member of the serralysin group characterized by a low optimal temperature.
Kumeta
H
H
Graduate School of Science and Engineering, Hokkaido Tokai University, Sapporo, Japan.
Hoshino
T
T
Goda
T
T
Okayama
T
T
Shimada
T
T
Ohgiya
S
S
Matsuyama
H
H
Ishizaki
K
K
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003080:Cold Temperature; D004269:DNA, Bacterial / Q000096:biosynthesis / Q000235:genetics; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D011551:Pseudomonas fluorescens / Q000378:metabolism*; D020449:Repetitive Sequences, Amino Acid / Q000502:physiology; D015032:Zinc / Q000378:metabolism
D004269:DNA, Bacterial; D008666:Metalloendopeptidases; C095666:serralysin; D015032:Zinc