Deletion of membrane‐associated Asp23 leads to upregulation of cell wall stress genes in Staphylococcus aureus. Issue 6 (19th August 2014)

• Record Type: Journal Article
• Authors: Müller, Marret; Reiß, Swantje; Schlüter, Rabea; Mäder, Ulrike; Beyer, Anica; Reiß, Wenke; Marles‐Wright, Jon; Lewis, Richard J.; Pförtner, Henrike; Völker, Uwe; Riedel, Katharina; Hecker, Michael; Engelmann, Susanne; Pané‐Farré, Jan
• Is Part Of: Molecular microbiology. Volume 93:Issue 6(2014)
• Page Start: 1259
• Page End: 1268
• Publication Date: 2014-08-19
• Subjects: Molecular microbiology -- Periodicals; 572.829
• DOI: 10.1111/mmi.12733
• Languages: English
• ISSNs: 0950-382X

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>With about 25 000 molecules per cell, Asp23 is one of the most abundant proteins in <italic>St</italic><italic>aphylococcus aureus</italic>. Asp23 has been characterized as a protein that, following an alkaline shock, accumulates in the soluble protein fraction. Transcription of the <italic>asp23</italic> 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 colocalized with the cell membrane of <italic>S</italic><italic>taphylococcus aureus</italic>. 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 <italic>asp23</italic> gene led to an upregulation 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.</p> </abstract>