Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme.
A 1.7-kb EcoRI fragment containing the structural gene for alpha-lytic protease has been cloned from Lysobacter enzymogenes 495 chromosomal DNA: the first example of a gene cloned from this organism. The protein sequence deduced from the nucleotide sequence encoding this serine protease matches the published amino acid sequence [Olson et al., Nature 228 (1970) 438-442] precisely. Sequence analysis and S1 mapping indicate that, like subtilisin [e.g., Wells et al., Nucleic Acids Res. 11 (1983) 7911-7925] alpha-lytic protease is synthesized as a pre-pro protein (41 kDa) that is subsequently processed to its mature extracellular form (20 kDa). This first finding of a large N-terminal protease precursor in a Gram-negative bacterial protease strengthens the hypothesis that large precursors may be a general property of extracellular bacterial proteases, and suggests that the N- or C-terminal location of the precursor segment may be significant.
Silen
J L
JL
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
McGrath
C N
CN
Smith
K R
KR
Agard
D A
DA
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon; D004792:Enzyme Precursors / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D006090:Gram-Negative Bacteria / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012697:Serine Endopeptidases / Q000235:genetics*
D003062:Codon; D004792:Enzyme Precursors; D012697:Serine Endopeptidases; C021826:myxobacter alpha-lytic proteinase