Open AccessConversion of the alpha component of penicillin-binding protein 1b to the beta component in Escherichia coli
Author(s) -
Hirotoshi Suzuki,
Junichi Kato,
Youji Sakagami,
Masashi Mori,
Ayano Suzuki,
Yukinori Hirota
Publication year - 1987
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.169.2.891-893.1987
Subject(s) - biology , penicillin binding proteins , beta (programming language) , amino acid , escherichia coli , peptide sequence , alpha (finance) , biochemistry , methionine , gene , microbiology and biotechnology , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
Among components alpha, beta, and gamma of penicillin-binding protein 1b, the alpha and gamma components were confirmed to represent the primary gene products by agreement of their N-terminal amino acid sequences with those predicted from the nucleotide sequence of the ponB (penicillin-binding protein 1b) gene with exclusion of the first methionine in each component. The generation of beta occurred primarily after cell disruption, and the simultaneous loss of alpha suggested the conversion of alpha to beta. The N-terminal amino acid sequence analyzed for beta showed that the conversion was due to the removal of 24 amino acids from the N terminus of alpha.