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Evolution of an inducible penicillin‐target protein in methicillin‐resistant Staphylococcus aureus by gene fusion
Author(s) -
Song Min Dong,
Wachi Masaaki,
Doi Masaki,
Ishino Fumitoshi,
Matsuhashi Michio
Publication year - 1987
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(87)80373-3
Subject(s) - penicillin binding proteins , staphylococcus aureus , gene , microbiology and biotechnology , penicillin , biology , nucleic acid sequence , escherichia coli , peptide sequence , fusion protein , antibiotics , bacteria , genetics , recombinant dna
A new β‐lactam‐inducible penicillin‐binding protein (PBP) that has extremely low affinity to penicillin and most other β‐lactam antibiotics has been widely found in highly, β‐lactam(methicillin)‐resistant Staphylococcus aureus (MRSA). The gene for this protein was sequenced and the nucleotide sequence in its promoter and close upstream area was found to show close similarity with that of staphylococcal penicillinase, while the amino acid sequence over a wide range of the molecule was found to be similar to those of two PBPs of Escherichia coli , the shape‐determining protein (PBP 2) and septum‐forming one (PBP 3). Probably the MRSA PBP ( M r 76462) evolved by recombination of two genes: an inducible type I penicillinase gene and a PBP gene of a bacterium, causing the formation of a β‐lactam‐inducible MRSA PBP.