Interaction of the cyclic-di-GMP binding protein FimX and the Type 4 pilus assembly ATPase promotes pilus assembly

Type IVa pili (T4P) are bacterial surface structures that enable motility, adhesion, biofilm formation and virulence. T4P are assembled by nanomachines that span the bacterial cell envelope. Cycles of T4P assembly and retraction, powered by the ATPases PilB and PilT, allow bacteria to attach to and...

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Bibliographic Details
Published in:	PLoS pathogens Vol. 13; no. 8; p. e1006594
Main Authors:	Jain, Ruchi, Sliusarenko, Oleksii, Kazmierczak, Barbara I.
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 30.08.2017 Public Library of Science (PLoS)
Subjects:	Adenosine triphosphatase Adhesion Adhesive strength Affinity Alleles Appendages (Animal anatomy) Assembly ATPases Bacteria Bacterial Proteins - metabolism Binding Binding proteins Biofilms Biology and Life Sciences Biosynthesis Carrier Proteins - metabolism Chromatography, Gel Cyclic GMP - analogs & derivatives Cyclic GMP - metabolism Deoxyribonucleic acid DNA Fimbriae, Bacterial - metabolism Gene mutation Genetic aspects Image Processing, Computer-Assisted In vitro methods and tests Infectious diseases Intracellular levels Intracellular Signaling Peptides and Proteins - metabolism Localization Medicine and Health Sciences Microscopy, Electron, Transmission Motility Oxidoreductases - metabolism Pathogenesis Pathogens Physiological aspects Pili Polymerase Chain Reaction Proteins Pseudomonas aeruginosa Pseudomonas aeruginosa - metabolism Research and Analysis Methods Surface Plasmon Resonance Tomography Twitching Virulence Virulence - physiology Virulence Factors - metabolism United States > US Connecticut
ISSN:	1553-7374, 1553-7366, 1553-7374
Online Access:	Get full text
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