Identification of three additional femAB-like open reading frames in Staphylococcus aureus

• Published in: FEMS microbiology letters Vol. 171; no. 2; pp. 97 - 102
• Main Authors: Tschierske, Martin, Mori, Claudio, Rohrer, Susanne, Ehlert, Kerstin, Shaw, Karen J., Berger-Bächi, Brigitte
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.02.1999; Blackwell; Oxford University Press
• Subjects: Antibiotics; Bacterial Proteins - genetics; Bacteriology; Biological and medical sciences; Cell Wall - metabolism; Chromosome Mapping; Chromosomes; Cloning, Molecular; Deactivation; DNA Probes; FemX; Fundamental and applied biological sciences. Psychology; Genetics; Genome, Bacterial; Genomes; Glycine; Inactivation; Lysostaphin; Methicillin resistance; Methicillin Resistance - genetics; Microbiology; Mutagenesis; Open reading frames; Open Reading Frames - genetics; Penicillin; Pentaglycine; Pentaglycine interpeptide; Peptidoglycan; Peptidoglycans; Proteoglycans - metabolism; Staphylococcus aureus; Staphylococcus aureus - genetics; Staphylococcus aureus - growth & development; Staphylococcus aureus - metabolism; Temperature; Peptidoglycan; Methicillin resistance; FemX; Pentaglycine interpeptide; Characterization; Gene; Bacteria; Micrococcales; Micrococcaceae; Biosynthesis; Cell wall; Staphylococcus aureus
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.1999.tb13417.x

Abstract Three new proteins, FmhA, FmhB and FmhC, with significant identities to FemA and FemB were identified in the Staphylococcus aureus (ATCC 55748) genome database. They were mapped to the SmaI-C, SmaI-H and SmaI-A fragments of the S. aureus 8325 chromosome, respectively. Whereas insertional inactivation of fmhA and fmhC had no effects on growth, antibiotic susceptibility, lysostaphin resistance, or peptidoglycan composition of the strains, fmhB could not be inactivated, strongly suggesting that fmhB may be an essential gene. As deduced from the functions of FemA and FemB which are involved in the synthesis of the peptidoglycan pentaglycine interpeptide, FmhB may be a candidate for the postulated FemX thought to add the first glycine to the nascent interpeptide.