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Cloning, purification and characterization of the collagenase ColA expressed by bacillus cereus ATCC 14579 / Carmen M. Abfalter, Esther Schönauer, Karthe Ponnuraj, Markus Huemer, Gabriele Gadermaier, Christof Regl, Peter Briza, Fatima Ferreira, Christian G. Huber, Hans Brandstetter, Gernot Posselt, Silja Wessler
VerfasserAbfalter, Carmen M. ; Schönauer, Esther ; Ponnuraj, Karthe ; Huemer, Markus ; Gadermaier, Gabriele ; Regl, Christof ; Briza, Peter In der Gemeinsamen Normdatei der DNB nachschlagen ; Ferreira, Fátima In der Gemeinsamen Normdatei der DNB nachschlagen ; Huber, Christian G. ; Brandstetter, Hans In der Gemeinsamen Normdatei der DNB nachschlagen ; Posselt, Gernot ; Wessler, Silja
Erschienen in
PLoS One, Lawrence, 2016, Jg. 11, S. 1-19
ErschienenPublic Library of Science, 2016
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
Schlagwörter (EN)Bacillus cereus / Collagenases / Proteases / Collagens / Signal peptides / Glutathione chromatography / Bacillus thuringiensis / Clostridium
URNurn:nbn:at:at-ubs:3-1495 Persistent Identifier (URN)
DOI10.1371/journal.pone.0162433 
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Cloning, purification and characterization of the collagenase ColA expressed by bacillus cereus ATCC 14579 [10.53 mb]
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Bacterial collagenases differ considerably in their structure and functions. The collagenases ColH and ColG from Clostridium histolyticum and ColA expressed by Clostridium perfringens are well-characterized collagenases that cleave triple-helical collagen, which were therefore termed as true collagenases. ColA from Bacillus cereus (B. cereus) has been added to the collection of true collagenases. However, the molecular characteristics of B. cereus ColA are less understood. In this study, we identified ColA as a secreted true collagenase from B. cereus ATCC 14579, which is transcriptionally controlled by the regulon phospholipase C regulator (PlcR). B. cereus ATCC 14579 ColA was cloned to express recombinant wildtype ColA (ColAwt) and mutated to a proteolytically inactive (ColAE501A) version. Recombinant ColAwt was tested for gelatinolytic and collagenolytic activities and ColAE501A was used for the production of a polyclonal anti-ColA antibody. Comparison of ColAwt activity with homologous proteases in additional strains of B. cereus sensu lato (B. cereus s.l.) and related clostridial collagenases revealed that B. cereus ATCC 14579 ColA is a highly active peptidolytic and collagenolytic protease. These findings could lead to a deeper insight into the function and mechanism of bacterial collagenases which are used in medical and biotechnological applications.

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