Cyclic diGMP regulates production of sortase substrates of Clostridium difficile and their surface exposure through ZmpI protease-mediated cleavage
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Published version
Accepted version
Author(s)
Type
Journal Article
Abstract
Background: Bacteria use various
mechanisms to anchor their surface proteins,
including a sortase enzyme.
Results: Covalent anchoring of proteins to the
peptidoglycan in Clostridium difficile and its
regulation by cyclic-di-GMP and protease
activity are demonstrated.
Conclusion: A novel regulatory mechanism of
cell wall protein anchoring is found.
Significance: Elucidating how proteins are
anchored may shed light on control of bacterial
colonization in vivo.
mechanisms to anchor their surface proteins,
including a sortase enzyme.
Results: Covalent anchoring of proteins to the
peptidoglycan in Clostridium difficile and its
regulation by cyclic-di-GMP and protease
activity are demonstrated.
Conclusion: A novel regulatory mechanism of
cell wall protein anchoring is found.
Significance: Elucidating how proteins are
anchored may shed light on control of bacterial
colonization in vivo.
Date Issued
2015-08-17
Date Acceptance
2015-08-17
Citation
Journal of Biological Chemistry, 2015, 290 (40), pp.24453-24469
ISSN
1083-351X
Publisher
American Society for Biochemistry and Molecular Biology
Start Page
24453
End Page
24469
Journal / Book Title
Journal of Biological Chemistry
Volume
290
Issue
40
Copyright Statement
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
Author's Choice—Final version free via Creative Commons CC-BY license http://creativecommons.org/licenses/by/3.0
Author's Choice—Final version free via Creative Commons CC-BY license http://creativecommons.org/licenses/by/3.0
License URL
Publication Status
Published