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You searched for: Subject "Listeria monocytogenes" Remove constraint Subject: "Listeria monocytogenes" Journal Journal of bacteriology Remove constraint Journal: Journal of bacteriology Publication Year 2015 Remove constraint Publication Year: 2015 Subject Listeria monocytogenes Remove constraint Subject: Listeria monocytogenes Subject pathogens Remove constraint Subject: pathogens Text Availability Full Text Remove constraint Text Availability: Full Text
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1. A prl Mutation in SecY Suppresses Secretion and Virulence Defects of Listeria monocytogenes secA2 Mutants

Author:
Durack, Juliana; Burke, Thomas P.; Portnoy, Daniel A.
Source:
Journal of bacteriology 2015 v.197 no.5 pp. 932-942
ISSN:
0021-9193
Subject:
Listeria monocytogenes,   etc   ; Gram-positive bacteria; adenosine triphosphate; adenosinetriphosphatase; bacterial motility; bacterial proteins; gametolysin; humans; hydrolysis; lysozyme; mice; mutants; operon; pathogenesis; pathogens; point mutation; protein secretion; sequence analysis; tissue culture; virulence;     Show all 20 Subjects
Abstract:
... The bulk of bacterial protein secretion occurs through the conserved SecY translocation channel that is powered by SecA-dependent ATP hydrolysis. Many Gram-positive bacteria, including the human pathogen Listeria monocytogenes , possess an additional nonessential specialized ATPase, SecA2. SecA2-dependent secretion is required for normal cell morphology and virulence in L. monocytogenes ; however, ...
DOI:
10.1128/JB.02284-14
PubMed:
25535272
PubMed Central:
PMC4325107

2. Interaction with Enzyme IIBᴹᵖᵒ (EIIBᴹᵖᵒ) and Phosphorylation by Phosphorylated EIIBᴹᵖᵒ Exert Antagonistic Effects on the Transcriptional Activator ManR of Listeria monocytogenes

Author:
Zébréé, Arthur Constant; Akééé, Francine Moussan; Ventroux, Magali; Koffi-Nevry, Rose; Noirot-Gros, Marie-Francoise; Deutscher, Josef; Milohanic, Eliane
Source:
Journal of bacteriology 2015 v.197 no.9 pp. 1559-1572
ISSN:
0021-9193
Subject:
Listeria monocytogenes,   etc   ; Listeria innocua; alleles; dephosphorylation; foodborne illness; gene expression; glucose; histidine; humans; listeriosis; mannose; mutants; operon; pathogens; phosphorylation; transcription (genetics); transcription factors; two hybrid system techniques; virulence;     Show all 19 Subjects
Abstract:
... Listeriae take up glucose and mannose predominantly through a mannose class phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS ᴹᵃⁿ), whose three components are encoded by the manLMN genes. The expression of these genes is controlled by ManR, a LevR-type transcription activator containing two PTS regulation domains (PRDs) and two PTS-like domains (enzyme IIA ᴹᵃⁿ [EIIA ᴹᵃⁿ]- and EIIB ᴳᵃ ...
DOI:
10.1128/JB.02522-14
PubMed:
25691525
PubMed Central:
PMC4403659