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The SLH‐domain protein BslO is a determinant of Bacillus anthracis chain length
Summary The Gram‐positive pathogen Bacillus anthracis grows in characteristic chains of individual, rod‐shaped cells. Here, we report the cell‐separating activity of BslO, a putative N‐acetylglucosaminidase bearing three N‐terminal S‐layer homology (SLH) domains for association with the secondary ce...
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Published in: | Molecular microbiology 2011-07, Vol.81 (1), p.192-205 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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The Gram‐positive pathogen Bacillus anthracis grows in characteristic chains of individual, rod‐shaped cells. Here, we report the cell‐separating activity of BslO, a putative N‐acetylglucosaminidase bearing three N‐terminal S‐layer homology (SLH) domains for association with the secondary cell wall polysaccharide (SCWP). Mutants with an insertional lesion in the bslO gene exhibit exaggerated chain lengths, although individual cell dimensions are unchanged. Purified BslO complements this phenotype in trans, effectively dispersing chains of bslO‐deficient bacilli without lysis and localizing to the septa of vegetative cells. Compared with the extremely long chain lengths of csaB bacilli, which are incapable of binding proteins with SLH‐domains to SCWP, bslO mutants demonstrate a chaining phenotype that is intermediate between wild‐type and csaB. Computational simulation suggests that BslO effects a non‐random distribution of B. anthracis chain lengths, implying that all septa are not equal candidates for separation. |
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ISSN: | 0950-382X 1365-2958 1365-2958 |
DOI: | 10.1111/j.1365-2958.2011.07688.x |