Browse by author
Lookup NU author(s): Dr Ulrike Mader, Wenke Reiss, Professor Rick Lewis
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).
With about 25000 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 sigma(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 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 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.
Author(s): Muller M, Reiss S, Schluter R, Mader U, Beyer A, Reiss W, Marles-Wright J, Lewis RJ, Pfortner H, Volker U, Riedel K, Hecker M, Engelmann S, Pane-Farre J
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Year: 2014
Volume: 93
Issue: 6
Pages: 1259-1268
Print publication date: 01/09/2014
Online publication date: 19/08/2014
Acceptance date: 29/07/2014
Date deposited: 11/07/2016
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: Wiley-Blackwell
URL: http://dx.doi.org/10.1111/mmi.12733
DOI: 10.1111/mmi.12733
Altmetrics provided by Altmetric
