Deletion of membrane-associated Asp23 leads to up-regulation of cell wall stress genes in Staphylococcus aureus

Marret Müller, Swantje Reiß, Rabea Schlüter, Ulrike Mäder, Anica Beyer, Wenke Reiß, Jon Marles-Wright, Richard J Lewis, Henrike Pförtner, Uwe Völker, Katharina Riedel, Michael Hecker, Susanne Engelmann, Jan Pané-Farré

Research output: Contribution to journalArticlepeer-review

Abstract

With about 25,000 molecules per cell, Asp23 is one of the most abundant proteins in Staphylococcus aureus. Asp23 has been characterized as a protein that, following an alkaline shock, accumulates in the soluble protein fraction. Transcription of the asp23 gene is exclusively regulated by the alternative sigma factor σ(B) , which controls the response of the bacterium to environmental stress. Sequence analysis identified Asp23 as a member of the widely distributed Pfam DUF322 family, precluding functional predictions based on its sequence. Using fluorescence microscopy we found that Asp23 co-localized with the cell membrane of Staphylococcus aureus. Since Asp23 has no recognizable transmembrane spanning domains, we initiated a search for proteins that link Asp23 to the cell membrane. We identified SAOUHSC_02443 as the Asp23 membrane anchor and have renamed it AmaP (Asp23 membrane anchoring protein). Deletion of the asp23 gene led to an up-regulation of the cell wall stress response. In summary, we have identified Asp23 as a membrane associated protein and we suggest a function for Asp23 in cell envelope homoeostasis.

Original languageEnglish
JournalMolecular Microbiology
DOIs
Publication statusPublished - 29 Jul 2014

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