Type IV pilus retraction in pathogenic Neisseria is regulated by the PilC proteins

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Type IV pilus retraction in pathogenic Neisseria is regulated by the PilC proteins.

Pathogenic Neisseria express type IV pili (tfp), which have been shown to play a central role in the interactions of bacteria with their environment. The regulation of piliation thus constitutes a central element in bacterial life cycle. The PilC proteins are outer membrane-associated proteins that have a key role in tfp biogenesis since PilC-null mutants appear defective for fibre expression. ...

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Fluctuations in type IV pilus retraction

The type IV pilus retraction motor is found in many important bacterial pathogens. It is the strongest known linear motor protein and is required for bacterial infectivity. We characterize the dynamics of type IV pilus retraction in terms of a stochastic chemical reaction model. We find that a two state model can describe the experimental force velocity relation and qualitative dependence of AT...

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Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Retraction of the type IV pilus (Tfp) mediates DNA uptake, motility, and social and infection behavior in a wide variety of prokaryotes. To date, investigations into Tfp retraction-dependent activities have used a mutant deleted of PilT, the ATPase motor protein that causes the pilus fiber to retract. ΔpilT cells are nontransformable, nonmotile, and cannot aggregate into microcolonies. We teste...

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Brownian motors in a ring and type IV pilus retraction

Motility of certain gram-negative bacteria is mediated by retraction of type IV pili surface filaments, which are essential for infectivity. The retraction is powered by a strong molecular motor protein, PilT, producing very high forces that exceed 100 pN (Maier, B., Potter, L., So, M., Seifert, H. S. and Sheetz, M. P., PNAS 99:16012 (2002)). In this paper we formulate a theoretical model for t...

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Structure of the Neisseria meningitidis Type IV pilus

Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin protein, which share a conserved hydrophobic N terminus that is a curved extended α-helix, α1, in X-ray crystal structures. Here we report a 1.44 Å crystal structure of the N. meningitidis major pilin...

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ژورنال

عنوان ژورنال: The EMBO Journal

سال: 2004

ISSN: 0261-4189,1460-2075

DOI: 10.1038/sj.emboj.7600200