In:
Molecular Microbiology, Wiley, Vol. 93, No. 6 ( 2014-09), p. 1259-1268
Abstract:
With about 25 000 molecules per cell, Asp 23 is one of the most abundant proteins in St aphylococcus aureus . Asp 23 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 Asp 23 as a member of the widely distributed P fam DUF 322 family, precluding functional predictions based on its sequence. Using fluorescence microscopy we found that Asp 23 colocalized with the cell membrane of S taphylococcus aureus . Since Asp 23 has no recognizable transmembrane spanning domains, we initiated a search for proteins that link Asp 23 to the cell membrane. We identified SAOUHSC _02443 as the Asp 23 membrane anchor and have renamed it AmaP ( Asp 23 membrane anchoring protein). Deletion of the asp23 gene led to an upregulation of the cell wall stress response. In summary, we have identified Asp 23 as a membrane‐associated protein and we suggest a function for Asp 23 in cell envelope homoeostasis.
Type of Medium:
Online Resource
ISSN:
0950-382X
,
1365-2958
DOI:
10.1111/mmi.2014.93.issue-6
Language:
English
Publisher:
Wiley
Publication Date:
2014
detail.hit.zdb_id:
1501537-3