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Role of the unique, non-essential phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) in Corynebacterium glutamicum.
Dautin, Nathalie; Argentini, Manuela; Mohiman, Niloofar; Labarre, Cécile; Cornu, David; Sago, Laila; Chami, Mohamed; Dietrich, Christiane; de Sousa d'Auria, Célia; Houssin, Christine; Masi, Muriel; Salmeron, Christophe; Bayan, Nicolas.
Afiliação
  • Dautin N; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Argentini M; Present address: Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, CNRS, Institut de Biologie Physico-Chimique, F-75005 Paris, France.
  • Mohiman N; Present address: Sorbonne Université, INSERM, CNRS, Institut de la Vision, 17 rue Moreau, 75012 Paris, France.
  • Labarre C; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Cornu D; Present address: Curakliniken, Erikslustvägen 22, 217 73 Malmö, Sweden.
  • Sago L; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Chami M; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Dietrich C; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • de Sousa d'Auria C; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Houssin C; CBioEM lab, Biozentrum, University of Basel, 4058 Basel, Switzerland.
  • Masi M; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Salmeron C; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
  • Bayan N; Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
Microbiology (Reading) ; 166(8): 759-776, 2020 08.
Article em En | MEDLINE | ID: mdl-32490790
ABSTRACT
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 phosphatidylglycerolprolipoprotein 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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Transferases / Corynebacterium glutamicum / Lipoproteínas Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Transferases / Corynebacterium glutamicum / Lipoproteínas Idioma: En Ano de publicação: 2020 Tipo de documento: Article