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J. Biol. Chem., Vol. 264, Issue 25, 14778-14783, 09, 1989
RW Soto-Gil and JW Zyskind
The nucleotide sequence of the gene, chb, encoding the outer membrane
protein, N,N'-diacetylchitobiase (chitobiase), of the marine bacterium,
Vibrio harveyi, has been determined. The amino acid sequence of
prechitobiase was derived from the nucleotide sequence. Prechitobiase has a
molecular mass of 97,771 Da and consists of 883 amino acid residues. A
characteristic signal peptide is present at the amino terminus whose
removal is inhibited by the antibiotic, globomycin, suggesting that mature
chitobiase is a lipoprotein with a maturation pathway similar to that of
the Escherichia coli major outer membrane lipoprotein. A perfect homology
to six amino acids at the processing and modification region of the outer
membrane lipoprotein of E. coli was found with amino acids 15-19 of the
deduced prechitobiase protein sequence. Chitobiase shares similarities and
possibly common ancestry with the alpha-chain of the human
beta-hexosaminidase. A comparison of the amino acid sequences of chitobiase
and the alpha-chain of beta- hexosaminidase gave a highly significant
alignment score of 19.1 standard deviation units above a mean randomized
alignment score. Primer extension analysis of the promoter region revealed
three transcription initiation sites used by E. coli cells harboring the
chb gene, two of which were also evident in V. harveyi cells.
N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing, and evolutionary relationships
Department of Biology, San Diego State University, California 92182.
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