@ARTICLE{TreeBASE2Ref26290,
author = {Maxime Mar?chal and Ana Amoroso and C?cile Morlot and Thierry Vernet and Jacques Coyette},
title = {Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site },
year = {2016},
keywords = {LCP, Psr, Enterococcus hirae, SCWP, peptidoglycan, septum},
doi = {},
url = {http://},
pmid = {},
journal = {BMC microbiology},
volume = {},
number = {},
pages = {},
abstract = {BACKGROUND: Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, here renamed LcpA, previously associated with the regulation of the expression of the low-affinity PBP5 and β-lactam resistance, has been characterized.
RESULTS: LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of secondary cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae.
CONCLUSIONS: LcpA belongs to the LytR-CpsA-Psr family. Its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.
}
}
Citation for Study 19821
Citation title:
"Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site ".
Study name:
"Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site ".
This study is part of submission 19821
(Status: Published).
Citation
Mar?chal M., Amoroso A., Morlot C., Vernet T., & Coyette J. 2016. Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site. BMC microbiology, .
Authors
-
Mar?chal M.
-
Amoroso A.
-
Morlot C.
-
Vernet T.
-
Coyette J.
Abstract
BACKGROUND: Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, here renamed LcpA, previously associated with the regulation of the expression of the low-affinity PBP5 and β-lactam resistance, has been characterized.
RESULTS: LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of secondary cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae.
CONCLUSIONS: LcpA belongs to the LytR-CpsA-Psr family. Its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.
Keywords
LCP, Psr, Enterococcus hirae, SCWP, peptidoglycan, septum
External links
About this resource
- Canonical resource URI:
http://purl.org/phylo/treebase/phylows/study/TB2:S19821
- Other versions:
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NeXML
- Show BibTeX reference
@ARTICLE{TreeBASE2Ref26290,
author = {Maxime Mar?chal and Ana Amoroso and C?cile Morlot and Thierry Vernet and Jacques Coyette},
title = {Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site },
year = {2016},
keywords = {LCP, Psr, Enterococcus hirae, SCWP, peptidoglycan, septum},
doi = {},
url = {http://},
pmid = {},
journal = {BMC microbiology},
volume = {},
number = {},
pages = {},
abstract = {BACKGROUND: Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, here renamed LcpA, previously associated with the regulation of the expression of the low-affinity PBP5 and β-lactam resistance, has been characterized.
RESULTS: LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of secondary cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae.
CONCLUSIONS: LcpA belongs to the LytR-CpsA-Psr family. Its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.
}
}
- Show RIS reference
TY - JOUR
ID - 26290
AU - Mar?chal,Maxime
AU - Amoroso,Ana
AU - Morlot,C?cile
AU - Vernet,Thierry
AU - Coyette,Jacques
T1 - Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site
PY - 2016
KW - LCP
KW - Psr
KW - Enterococcus hirae
KW - SCWP
KW - peptidoglycan
KW - septum
UR - http://dx.doi.org/
N2 - BACKGROUND: Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, here renamed LcpA, previously associated with the regulation of the expression of the low-affinity PBP5 and β-lactam resistance, has been characterized.
RESULTS: LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of secondary cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae.
CONCLUSIONS: LcpA belongs to the LytR-CpsA-Psr family. Its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.
L3 -
JF - BMC microbiology
VL -
IS -
ER -
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