tatA Antibody

1. The authors observe that substitutions of charged residues located in the TatA amphipathic helix lock TatA in an assembled state, suggesting that these charged residues play a critical role in the protein translocation step that follows TatA assembly. PMID: 28857741
2. Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. PMID: 24003141
3. Each subunit of TatA consists of a transmembrane segment, an amphiphilic helix (APH), and a C-terminal densely charged region (DCR). The sequence of charges in the DCR is complementary to the charge pattern on the APH, suggesting that the protein can be "zipped up" by a ladder of seven salt bridges. PMID: 23332763
4. analysis of the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli PMID: 21683683
5. the TatA protein represents a bifunctional component fulfilling both the TatA and TatB functions. PMID: 15557327
6. TatA fused to green/cyan/yellow fluorescent protein is found to be preferentially incorporated into the TatABC complex. PMID: 15728576
7. TatA may be the major pore-forming subunit in the twin-arginine translocation pathway [review] PMID: 15748976
8. We used purified preproteins to study interaction with the phospholipid membrane by using surface plasmon resonance.Preproteins interact tightly with a model membrane consisting of only phospholipids in early step in protein translocation by Tat system. PMID: 16475812
9. it is only in TatA that the amphipathic helix is sensitive to amino acid substitutions; the TatA amphipathic helix may play a role in forming and controlling the path of substrate movement across the membrane PMID: 17565984
10. data support the TatA polymerization model for the mechanism of Tat transport. PMID: 18832162

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KEGG: ecj:JW3813

STRING: 316385.ECDH10B_4027