Cloning and sequencing of beta-1,4-endoglucanase gene (celA) from Pseudomonas sp. YD-15.
A beta-1,4-endoglucanase gene (celA) from Pseudomonas sp. YD-15 was cloned in Escherichia coli DH5 alpha and its nucleotide sequence determined. The open reading frame of celA was 1830 base pairs and the enzyme was composed of 609 amino acids with a molecular weight of 63,617 Da. The deduced amino acid sequence and putative active site of CelA had high amino acid homology with family E cellulases. By dot blot analysis, the induction of celA according to carbon sources was determined. The transcripts hybridizing to the internal fragment of celA were detected in total RNA isolated from Pseudomonas sp. YD-15 cells grown on avicel and glycerol, but not from cells grown on glucose and cellobiose.
Her
S
S
Department of Biotechnology, College of Engineering and Bioproducts Research Center, Yonsei University, Seoul, Korea. song_her@hms.harvard.edu
Lee
H S
HS
Choi
S J
SJ
Choi
S W
SW
Choi
H J
HJ
Yoon
S S
SS
Oh
D H
DH
D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D002480:Cellulase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003001:Cloning, Molecular; D003470:Culture Media; D017353:Gene Deletion; D008969:Molecular Sequence Data; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D015183:Restriction Mapping; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D003470:Culture Media; C074775:CelA endoglucanase; D002480:Cellulase