Role of the unique, non-essential phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) in; Corynebacterium glutamicum;

Dautin, Nathalie and Argentini, Manuela and Mohiman, Niloofar and Labarre, Cécile and Cornu, David and Sago, Laila and Chami, Mohamed and Dietrich, Christiane and de Sousa d'Auria, Célia and Houssin, Christine and Masi, Muriel and Salmeron, Christophe and Bayan, Nicolas. (2020) Role of the unique, non-essential phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) in; Corynebacterium glutamicum;. Microbiology, 166 (8). pp. 759-776.

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Official URL: https://edoc.unibas.ch/78618/

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Bacterial lipoproteins are secreted proteins that are post-translationally lipidated. Following synthesis, preprolipoproteins are transported through the cytoplasmic membrane via the Sec or Tat translocon. As they exit the transport machinery, they are recognized by a phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt), which converts them to prolipoproteins by adding a diacylglyceryl group to the sulfhydryl side chain of the invariant Cys; +1; residue. Lipoprotein signal peptidase (LspA or signal peptidase II) subsequently cleaves the signal peptide, liberating the α-amino group of Cys; +1; , which can eventually be further modified. Here, we identified the; lgt; and; lspA; genes from; Corynebacterium glutamicum; and found that they are unique but not essential. We found that Lgt is necessary for the acylation and membrane anchoring of two model lipoproteins expressed in this species: MusE, a; C. glutamicum; maltose-binding lipoprotein, and LppX, a; Mycobacterium tuberculosis; lipoprotein. However, Lgt is not required for these proteins' signal peptide cleavage, or for LppX glycosylation. Taken together, these data show that in; C. glutamicum; the association of some lipoproteins with membranes through the covalent attachment of a lipid moiety is not essential for further post-translational modification.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
UniBasel Contributors:Chami, Mohamed
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Microbiology Society
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:26 Jan 2022 13:31
Deposited On:26 Jan 2022 13:31

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