SITE-DIRECTED MUTAGENESIS OF THE MECA GENE FROM A METHICILLIN-RESISTANT STRAIN OF STAPHYLOCOCCUS-AUREUS

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WU C., ALBORN W., FLOKOWITSCH J., HOSKINS J., UNAL S., BLASZCZAK L., ...Daha Fazla

JOURNAL OF BACTERIOLOGY, cilt.176, sa.2, ss.443-449, 1994 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 176 Sayı: 2
  • Basım Tarihi: 1994
  • Doi Numarası: 10.1128/jb.176.2.443-449.1994
  • Dergi Adı: JOURNAL OF BACTERIOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.443-449
  • Hacettepe Üniversitesi Adresli: Evet

Özet

The mecA-27r gene from Staphylococcus aureus 27r encodes penicillin-binding protein 2a (PBP2a-27r), which causes this strain to be methicillin resistant. Removal or replacement of the N-terminal transmembrane domain had no effect on binding of penicillin, but removal of portions of the putative transglycosylase domain (144, 245, or 341 amino acids after the transmembrane region) destroyed penicillin-binding activity. The SXXK, SXN, and KSG motifs, present in all penicillin-interacting enzymes, were found in the expected linear spatial arrangement within the putative transpeptidase region of PBP2a-27r. Alterations of amino acids in all three of these motifs resulted in elimination of penicillin-binding activity, confirming their roles in the interaction with penicillin.