Zobrazeno 1 - 10
of 161
pro vyhledávání: '"Anthony P. Pugsley"'
Autor:
Hanh H. Hoang, Nicholas N. Nickerson, Vincent T. Lee, Anastasia Kazimirova, Mohamed Chami, Anthony P. Pugsley, Stephen Lory
Publikováno v:
mBio, Vol 2, Iss 6 (2011)
ABSTRACT In Gram-negative bacteria, the Lol and Bam machineries direct the targeting of lipidated and nonlipidated proteins, respectively, to the outer membrane (OM). Using Pseudomonas aeruginosa strains with depleted levels of specific Bam and Lol p
Externí odkaz:
https://doaj.org/article/0f33d4338785498a93ba3cff11727507
Autor:
Mohamed Chami, Julia Chamot-Rooke, Sébastien Brier, Gerard H. M. Huysmans, Véronique Hourdel, Ingrid Guilvout, Anthony P. Pugsley, Olivera Francetic
Publikováno v:
Journal of Biological Chemistry. 292:328-338
Members of a group of multimeric secretion pores that assemble independently of any known membrane-embedded insertase in Gram-negative bacteria fold into a prepore before membrane-insertion occurs. The mechanisms and the energetics that drive the fol
Autor:
Anthony P. Pugsley, Andréa Dessen, Ingrid Guilvout, Tommaso Tosi, Viviana Job, Guy Schoehn, Leandro F. Estrozi
Publikováno v:
Structure
Structure, 2014, 22 (9), pp.1348-1355. ⟨10.1016/j.str.2014.07.005⟩
Structure, Elsevier (Cell Press), 2014, 22 (9), pp.1348-1355. ⟨10.1016/j.str.2014.07.005⟩
Structure, 2014, 22 (9), pp.1348-1355. ⟨10.1016/j.str.2014.07.005⟩
Structure, Elsevier (Cell Press), 2014, 22 (9), pp.1348-1355. ⟨10.1016/j.str.2014.07.005⟩
International audience; Secretins, the outer membrane components of several secretion systems in Gram-negative bacteria, assemble into channels that allow exoproteins to traverse the membrane. The membrane-inserted, multimeric regions of PscC, the Ps
Autor:
Nicolas Bayan, Gerard H. M. Huysmans, Mohamed Chami, Anthony P. Pugsley, Elena Disconzi, Ingrid Guilvout, Muriel Masi
Publikováno v:
Journal of Bacteriology. 196:121-128
Proteins called secretins form large multimeric complexes that are essential for macromolecular transit across the outer membrane of Gram-negative bacteria. Evidence suggests that the channels formed by some secretin complexes are not tightly closed,
Autor:
Mohamed Chami, Anthony P. Pugsley, Nicholas N. Nickerson, Eduardo P. C. Rocha, Sophie S. Abby
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 2012, 194 (18), pp.4951-4958. ⟨10.1128/JB.00798-12⟩
Journal of Bacteriology, 2012, 194 (18), pp.4951-4958. ⟨10.1128/JB.00798-12⟩
Journal of Bacteriology, American Society for Microbiology, 2012, 194 (18), pp.4951-4958. ⟨10.1128/JB.00798-12⟩
Journal of Bacteriology, 2012, 194 (18), pp.4951-4958. ⟨10.1128/JB.00798-12⟩
Secretins form large multimeric complexes in the outer membranes of many Gram-negative bacteria, where they function as dedicated gateways that allow proteins to access the extracellular environment. Despite their overall relatedness, different secre
Autor:
Peter J. Bond, Pedro M. Alzari, Alexandra East, Ariel E. Mechaly, Alejandro Buschiazzo, Nathalie Nadeau, Olivera Francetic, Gerard H. M. Huysmans, Diana Tello-Manigne, Anthony P. Pugsley, Cédric Bernarde
Publikováno v:
Structure
Structure, Elsevier (Cell Press), 2016, 24 (1), pp.92-104. ⟨10.1016/j.str.2015.10.023⟩
Structure, 2016, 24 (1), pp.92-104. ⟨10.1016/j.str.2015.10.023⟩
Structure, Elsevier (Cell Press), 2016, 24 (1), pp.92-104. ⟨10.1016/j.str.2015.10.023⟩
Structure, 2016, 24 (1), pp.92-104. ⟨10.1016/j.str.2015.10.023⟩
International audience; The Klebsiella lipoprotein pullulanase (PulA) is exported to the periplasm, triacylated, and anchored via lipids in the inner membrane (IM) prior to its transport to the bacterial surface through a type II secretion system (T2
Publikováno v:
The EMBO Journal. 31:1041-1053
In Gram-negative bacteria, type II secretion systems (T2SS) assemble inner membrane proteins of the major pseudopilin PulG (GspG) family into periplasmic filaments, which could drive protein secretion in a piston-like manner. Three minor pseudopilins
Publikováno v:
Molecular Microbiology. 80:655-665
Summary The lipoprotein PulS is a dedicated chaperone that is required to target the secretin PulD to the outer membrane in Klebsiella or Escherichia coli, and to protect it from proteolysis. Here, we present indirect evidence that PulD protomers do
Autor:
Mohamed Chami, Ingrid Guilvout, Alexandre Ghazi, Anthony P. Pugsley, Catherine Berrier, Nicolas Bayan, Agnes Mesneau, Kyu-Ho Park
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1808(1):41-46
The mechanosensitive channel MscL of the plasma membrane of bacteria is a homopentamer involved in the protection of cells during osmotic downshock. The MscL protein, a polypeptide of 136 residues, was recently shown to require YidC to be inserted in
Publikováno v:
Journal of Bacteriology. 190:6119-6125
The ultimate membrane localization and function of most of the 185 predicted Pseudomonas aeruginosa PAO1 lipoproteins remain unknown. We constructed a fluorescent lipoprotein, CSFP OmlA -ChFP, by fusing the signal peptide and the first four amino aci