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Bacillus cereus 569/H β‐lactamase I: Cloning in Escherichia coli and signal sequence determination
Author(s) -
Mézes Peter S.F.,
Yang Yue Qin,
Hussain Musaddeq,
Oliver Lampen J.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81006-0
Subject(s) - bacillus cereus , escherichia coli , bacillus licheniformis , cereus , signal peptide , biology , peptide sequence , microbiology and biotechnology , bacillaceae , open reading frame , nucleic acid sequence , biochemistry , chemistry , gene , bacteria , bacillus subtilis , genetics
The gene, penPC , for β‐lactamase I of Bacillus cereus 569/H has been cloned and its expression studied in Escherichia coli . The protein product from the in vitro translation of penPC was shown by gel electrophoresis to have an M r of 36 000 which is larger than the in vivo products fround in B. cereus and E. coli . The DNA sequence of the signal region was determined. It revealed that the smallest known mature form present in B. cereus culture fluids is preceded by 45–48 amino acids in pre‐β‐lactamase I, considering that there are 3 initiation codons in the same reading frame, one or more of which might be initiating translation. Unlike the Bacillus licheniformis 749/C β‐lactamase, which has a membrane‐bound thioether lipoprotein form, the single Cys residue in the B. cereus β‐lactamase I signal sequence is unmodified and a single processed form of the enzyme is present in E. coli cells carrying pen PC