tatB Antibody

1. It has been concluded that Tat signal peptides play roles in substrate targeting and in triggering assembly of the active TatABC translocase. PMID: 28223511
2. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, the authors find that TatA also associates with TatC at the polar cluster site. PMID: 27914200
3. In vitro cross-linking of residues located in the periplasmically-oriented part of the TatBC receptor to TorA[KQ]-30aa-MalE reporter variants harboring a more hydrophobic h-region in their signal peptides confirmed that unlike in TorA[KQ]-30aa-MalE with an unaltered h-region, the mutated reporters moved deep into the TatBC-binding cavity. PMID: 28515319
4. Twin-arginine translocation (Tat) system TatA exhibits a uniform distribution throughout the inner membrane and that altering the expression of TatBC shows a uncharacterised distribution of TatA in the inner membrane. PMID: 28280110
5. we confirm the evidence of interactions between TatC fragments and DmsD chaperone. Using a peptide overlapping array, it was shown that the different NarJ subfamily REMPs interact with different regions of the TatB cytoplasmic domains PMID: 26826271
6. Distributed TatA thus may serve to accompany membrane-interacting Tat substrates to the few TatBC spots in the cells. PMID: 25774531
7. The data thus suggest that mature protein domains are translocated through a TatA and TaTB environment. PMID: 25003386
8. A physical interaction between TatC helix 5 and the TatB transmembrane helix was confirmed by the formation of a site-specific disulphide bond between TatC M205C and TatB L9C variants. PMID: 22742417
9. The transmembrane helix of TatA makes contacts with TatC and precursors recognized by the TatBC complex PMID: 22041896
10. data are consistent with TatB forming an oligomeric binding site that transiently accommodates folded Tat precursors PMID: 20926683
11. findigs show the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein; truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised PMID: 21237157
12. Data show that homo- and hetero-oligomeric complexes of the TatA, TatB and TatC integral membrane proteins were consistent with the current model of translocase assembly. PMID: 20169075
13. the TatABC complex of the twin-arginine translocase in Escherichia coli has specific roles in assembly and stability PMID: 15571732
14. the data indicate the presence of an additional form of Tat complex containing TatA and TatB, but not TatC PMID: 15663945
15. Since TatC is invariably complexed with TatB in wild-type complexes, the combined data demonstrate that TatABC complexes are uniformly distributed throughout the E. coli plasma membrane. PMID: 15728576
16. Data show that the integrity of the TatA TM span is vital for Tat activity, whereas that of TatB can accommodate large-scale distortions and only substitutions of P48 and F94 in TatC blocks activity. PMID: 15853811
17. analysis of substrate specificity of the TatB and TatC translocases with the consensus motif of a Tat signal peptide PMID: 17229735
18. tatABC and tatAC expression has a role in the formation of interacting cytoplasmic TatA tubes in Escherichia coli PMID: 18644791

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KEGG: ecj:JW5580

STRING: 316385.ECDH10B_4028