Title |
The ppm Operon Is Essential for Acylation and Glycosylation of Lipoproteins in Corynebacterium glutamicum
|
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Published in |
PLOS ONE, September 2012
|
DOI | 10.1371/journal.pone.0046225 |
Pubmed ID | |
Authors |
Niloofar Mohiman, Manuela Argentini, Sarah M. Batt, David Cornu, Muriel Masi, Lothar Eggeling, Gurdyal Besra, Nicolas Bayan |
Abstract |
Due to their contribution to bacterial virulence, lipoproteins and members of the lipoprotein biogenesis pathway represent potent drug targets. Following translocation across the inner membrane, lipoprotein precursors are acylated by lipoprotein diacylglycerol transferase (Lgt), cleaved off their signal peptides by lipoprotein signal peptidase (Lsp) and, in Gram-negative bacteria, further triacylated by lipoprotein N-acyl transferase (Lnt). The existence of an active apolipoprotein N-acyltransferase (Ms-Ppm2) involved in the N-acylation of LppX was recently reported in M. smegmatis. Ms-Ppm2 is part of the ppm operon in which Ppm1, a polyprenol-monophosphomannose synthase, has been shown to be essential in lipoglycans synthesis but whose function in lipoprotein biosynthesis is completely unknown. |
X Demographics
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Scientists | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 48 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 12 | 25% |
Student > Master | 9 | 19% |
Researcher | 8 | 17% |
Student > Bachelor | 5 | 10% |
Professor | 3 | 6% |
Other | 6 | 13% |
Unknown | 5 | 10% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 18 | 38% |
Biochemistry, Genetics and Molecular Biology | 14 | 29% |
Chemistry | 4 | 8% |
Medicine and Dentistry | 3 | 6% |
Immunology and Microbiology | 2 | 4% |
Other | 1 | 2% |
Unknown | 6 | 13% |