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Tight junction associated protein 1

This gene encodes a tight junction-associated protein. Incorporation of the encoded protein into tight junctions occurs at a late stage of formation of the junctions. The encoded protein localizes to the Golgi and may function in vesicle trafficking. Alternatively spliced transcript variants have been described. A related pseudogene exists on the X chromosome. [provided by RefSeq, Mar 2009] (from NCBI)
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Top mentioned proteins: TFP, CAN, ATPase, ACID, PIN
Papers on PilT
PilB localization correlates with the direction of twitching motility in the cyanobacterium Synechocystis sp. PCC 6803.
Wilde et al., Freiburg, Germany. In Microbiology, May 2015
In M. xanthus, the direction of movement depends on the unipolar localization of the pilus extension and retraction motors PilB and PilT to opposite cell poles.
Calcium-Enhanced Twitching Motility in Xylella fastidiosa Is Linked to a Single PilY1 Homolog.
De La Fuente et al., Auburn, United States. In Appl Environ Microbiol, 2014
Ca does not modulate the expression of any of the X. fastidiosa PilY1 homologs, although it increases the expression of the retraction ATPase pilT during active movement.
Characterization of motility and piliation in pathogenic Neisseria.
Jonsson et al., Stockholm, Sweden. In Bmc Microbiol, 2014
Tfp retraction, which is dependent on the ATPase PilT, generates the forces that move bacteria over surfaces.
Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly.
Srinivasan et al., New Delhi, India. In J Struct Biol, 2014
Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown.
Efficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicus.
Shen et al., Jinan, China. In Bmc Mol Biol, 2014
NurA and two other putative HRR proteins: a PIN (PilT N-terminal)-domain containing ATPase and the Holliday junction resolvase Hjc, were co-purified with a chromosomally encoded N-His-HerA in vivo.
Hypervariable pili and flagella genes provide suitable new targets for DNA high-resolution melt-based genotyping of dairy Geobacillus spp.
Turner et al., Brisbane, Australia. In J Food Prot, 2014
Three genes encoding pulG (containing prepilin-type N-terminal cleavage domain), pilT (pili retraction protein), and fliW (flagellar assembly protein) were selected as targets for the new pili/flagella gene (PilFla) HRMA genotyping method.
Type-IV Pilus deformation can explain retraction behavior.
Vaziri et al., Edmonton, Canada. In Plos One, 2013
Single TFP level experiments have shown remarkable nonlinearity in the retraction behavior influenced by the external load as well as levels of PilT molecular motor protein.
Role of type IV pili in predation by Bdellovibrio bacteriovorus.
Koval et al., London, Canada. In Plos One, 2013
In other bacteria, these pili have the ability to extend and retract via the PilT protein.
MCP-1-induced protein-1, an immune regulator.
Rao et al., Beijing, China. In Protein Cell, 2012
The structure of MCPIP1 N-terminal conserved domain shows a PilT N-terminus-like RNase structure, further supporting the notion that MCPIP1 has RNase activity.
The pathogenesis of ovine footrot.
Rood et al., Australia. In Vet Microbiol, 2011
Mutagenesis of the fimbrial subunit gene fimA and the pilT gene, which is required for fimbrial retraction, and subsequent testing of these mutants in sheep virulence trials has shown that type IV fimbriae-mediated twitching motility is essential for virulence.
Structure and function of the 5'-->3' exoribonuclease Rat1 and its activating partner Rai1.
Tong et al., New York City, United States. In Nature, 2009
There are large differences in the active site landscape of Rat1 compared to related and PIN (PilT N terminus) domain-containing nucleases.
Type II secretion and type IV pili of Francisella.
Guina et al., UmeƄ, Sweden. In Ann N Y Acad Sci, 2007
In contrast, type B strains show several differences compared to type A strains, two predicted pilin genes and the pilT gene are pseudogenes, while pilA is identical to pilA that is encoded by the type A strains.
The PIN-domain toxin-antitoxin array in mycobacteria.
Turner et al., Auckland, New Zealand. In Trends Microbiol, 2005
PIN-domains (homologues of the pilT N-terminal domain) are small protein domains of approximately 140 amino acids.
STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer.
Aravind et al., Bethesda, United States. In J Mol Biol, 2004
The STAND class belongs to the additional strand, catalytic E division of P-loop NTPases together with the AAA+ ATPases, RecA/helicase-related ATPases, ABC-ATPases, and VirD4/PilT-like ATPases.
Pilus retraction powers bacterial twitching motility.
Sheetz et al., Portland, United States. In Nature, 2000
Both motility and retraction mediated by Tfp occur at about 1 microm s(-1) and require protein synthesis and function of the PilT protein.
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