The Twin-arginine Signal Peptide of PhoD and the TatAd/Cd Proteins of Bacillus subtilis Form an Autonomous Tat Translocation System

Pop, Ovidiu I.; Martin, Ulrike; Abel, Christian; Müller, Jörg P.

doi:10.1074/jbc.m110829200

Cited by 97 publications

(82 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Some gram-positive bacteria and archaea contain multiple tatC genes as well as multiple tatA/B genes. For example, Bacillus subtilis has two tatC genes (and three tatA genes) (75), each of which seems to constitute separate, substrate-specific Tat systems (73,74,99).…”

Section: Tm: Transmembranementioning

confidence: 99%

The Bacterial Twin-Arginine Translocation Pathway

Lee

Tullman‐Ercek

Georgiou

2006

Annu. Rev. Microbiol.

296

241

View full text Add to dashboard Cite

The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria. Substrates for the Tat pathway include redox enzymes requiring cofactor insertion in the cytoplasm, multimeric proteins that have to assemble into a complex prior to export, certain membrane proteins, and proteins whose folding is incompatible with Sec export. These proteins are involved in a diverse range of cellular activities including anaerobic metabolism, cell envelope biogenesis, metal acquisition and detoxification, and virulence. The Escherichia coli translocase consists of the TatA, TatB, and TatC proteins, but little is known about the precise sequence of events that leads to protein translocation, the energetic requirements, or the mechanism that prevents the export of misfolded proteins. Owing to the unique characteristics of the pathway, it holds promise for biotechnological applications.

show abstract

Section: Tm: Transmembranementioning

confidence: 99%

The Bacterial Twin-Arginine Translocation Pathway

Lee

Tullman‐Ercek

Georgiou

2006

Annu. Rev. Microbiol.

296

241

View full text Add to dashboard Cite

show abstract

“…The TatAdCd and TatAyCy translocases have different but overlapping specificities, and their usage is strongly dependent on growth conditions. Under conditions of phosphate starvation, the TatAdCd translocase is responsible for secretion of the phosphodiesterase PhoD, whereas TatAyCy is dispensable for this process (25,39). Conversely, when cells are cultivated in the standard Luria-Bertani (LB) medium, the TatAyCy translocase secretes the Dyp-type peroxidase YwbN without any detectable involvement of TatAdCd (28,40).…”

mentioning

confidence: 99%

Salt Sensitivity of Minimal Twin Arginine Translocases

Ploeg

Barnett

Vasisht

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Minimal twin arginine preprotein translocases consist of TatA and TatC subunits. Results: Here we show that various mutated and wild-type minimal Tat translocases are salt-sensitive. Conclusion: Salt-sensitive electrostatic interactions seem to have critical roles in the preprotein translocation activity of minimal Tat translocases. Significance: Our results represent first experimental evidence for an important role of salt-sensitive electrostatic interactions in Tat translocation.

show abstract

“…The mechanism of this transport is unknown but must be quite unusual, because the transported proteins can be even larger in diameter than the membrane they are transported across (2). The minimal Tat translocon is composed of two components, TatA and TatC (3,4). Proteobacteria and thylakoids require a third component for efficient translocation, TatB, which associates with TatC to form a TatBC complex (1).…”

mentioning

confidence: 99%

Recombinant Expression of tatABC and tatAC Results in the Formation of Interacting Cytoplasmic TatA Tubes in Escherichia coli

Berthelmann

Mehner

Richter

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

The twin-arginine translocation (Tat) system of bacteria and plant plastids serves to translocate folded proteins across energized biological membranes. In Escherichia coli, the three components TatA, TatB, and TatC mediate this membrane passage. Here we demonstrate that TatA can assemble to form clusters of tube-like structures in vivo. While the presence of TatC is essential for their formation, TatB is not required. The TatA tubes have uniform outer and inner diameters of about 11.5 nm and 6.7 nm, respectively. They align to form a crystalline-like structure in which each tube is surrounded by six TatA tubes. The tube structures become easily detectable even at only a 15-fold overexpression of the tatABC genes. The TatA tubes could also be visualized by fluorescence when untagged TatA was mixed with low amounts of TatA-GFP. The structures were often found in contact with the cell poles. Because TatC is most likely polar in E. coli, as demonstrated by a RR-dependent targeting of translocation-incompatible Tat substrates to the cell poles, and because TatC is required for the formation of aligned TatA tubes, it is proposed that the TatA tubes are initiated at polarly localized TatC.Folded proteins can be transported across membranes by the twin-arginine translocation (Tat) 3 system (1). The mechanism of this transport is unknown but must be quite unusual, because the transported proteins can be even larger in diameter than the membrane they are transported across (2). The minimal Tat translocon is composed of two components, TatA and TatC (3, 4). Proteobacteria and thylakoids require a third component for efficient translocation, TatB, which associates with TatC to form a TatBC complex (1). Because Tat substrates bind tightly only to TatBC complexes, and because a covalent cross-link to TatC still allows translocation, it is believed that TatC is the motor for the translocation process (5). TatA, however, also plays an essential role, most likely by allowing the membrane passage of the substrate, which is moved by TatC across the membrane (6). TatA is also the most abundant Tat component in Escherichia coli (7). In the chloroplast system, the association of TatA with the TatBC complex occurs strictly after substrate binding (6), whereas TatA of Gram-positive bacteria has been detected inside the cytoplasm, where it has a high affinity for Tat substrates that might be targeted by TatA to the membranes (8 -10). TatA of the E. coli Tat system is known to form homooligomeric complexes (11). It has been purified from detergent-solubilized membrane fractions of strains overexpressing the tatABC genes (12). The TatA complexes identified in that study varied in diameter and formed a ladder in blue native polyacrylamide gel electrophoresis (BN-PAGE) analyses. The variable sizes of these TatA complexes suggest the existence of some higher order homooligomeric TatA structure, which might have been disrupted by detergent treatment. We therefore analyzed strains overexpressing tatABC, tatAB, tatAC, or tatA by transmission...

show abstract

The Twin-arginine Signal Peptide of PhoD and the TatAd/Cd Proteins of Bacillus subtilis Form an Autonomous Tat Translocation System

Cited by 97 publications

References 39 publications

The Bacterial Twin-Arginine Translocation Pathway

The Bacterial Twin-Arginine Translocation Pathway

Salt Sensitivity of Minimal Twin Arginine Translocases

Recombinant Expression of tatABC and tatAC Results in the Formation of Interacting Cytoplasmic TatA Tubes in Escherichia coli

Contact Info

Product

Resources

About