Soluble TatA forms oligomers that interact with membranes: Structure and insertion studies of a versatile protein transporter

Pettersson, Per; Patrick, Joan; Jakob, Mario; Jacobs, M H; Klösgen, Ralf Bernd; Wennmalm, Stefan; Mäler, Lena

doi:10.1016/j.bbamem.2020.183529

Cited by 8 publications

(11 citation statements)

References 34 publications

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“…However, examples of short peptides integrating into both artificial and biological membranes are known from the literature 53 , 54 , 55 . In addition, several studies have shown that soluble TatA is able to be functionally incorporated into thylakoid membranes ( 20 , 36 , 56 , 57 , 58 , 59 ). The TatB Bd4 mutant loses its membrane location in the absence of TatC ( Fig.…”

Section: Discussionmentioning

confidence: 99%

Hydrophobic mismatch is a key factor in protein transport across lipid bilayer membranes via the Tat pathway

Hao

Zhou

Theg

2022

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Hydrophobic mismatch is a key factor in protein transport across lipid bilayer membranes via the Tat pathway

Hao

Zhou

Theg

2022

Journal of Biological Chemistry

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“…It is perhaps unexpected that the deletion mutants as short as 11 residues were still able to take up residence in the membranes and resist extraction by carbonate. However, examples of short peptides integrating into both artificial and biological membranes are known from the literature (Ulmschneider et al 2018; de Planque et al 2003; Jaud et al 2009) Additionally, several studies have shown that soluble TatA is able to be functionally incorporated into thylakoid membranes (Aldridge et al, 2012; Dabney-Smith et al, 2006, 2003; Frielingsdorf et al, 2008; Hauer et al, 2013; Pettersson et al, 2021). The TatB Bd4 mutant loses its membrane location in the absence of TatC (Figure 4C), which points to a stabilizing interaction between the short TatB and TatC.…”

Section: Discussionmentioning

confidence: 99%

Hydrophobic mismatch is a key factor in protein transport on the Tat pathway

Hao

Zhou

2021

Preprint

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The twin-arginine translocation (Tat) pathway transports folded proteins across membranes in bacteria, thylakoid, plant mitochondria, and archaea. In most species, the active Tat machinery consists of three independent subunits, TatA, TatB and TatC. TatA and TatB from all bacterial species possess short transmembrane alpha-helices (TMHs), both of which are only fifteen residues long in E. coli. Such short TMHs cause a hydrophobic mismatch between Tat subunits and the membrane bilayer. Here, by modifying the length of the TMHs of E. coli TatA and TatB, we access the functional importance of the hydrophobic mismatch in the Tat transport mechanism. Surprisingly, both TatA and TatB with as few as 11 residues in their respective TMHs are still able to insert into the membrane bilayer, albeit with a decline in membrane integrity. Three different assays, both qualitative and quantitative, were conducted to evaluate the Tat activity of the TMH length mutants. Our experiments indicate that the TMHs of TatA and TatB appear to be evolutionarily tuned to 15 amino acids, with activity dropping off with any modification of this length. We believe our study supports a model of Tat transport utilizing localized toroidal pores that form when the membrane bilayer is thinned to a critical threshold. In this context, the 15-residue length of the TatA and TatB TMHs can be seen as a compromise between the need for some hydrophobic mismatch to allow the membrane to reversibly reach the threshold thinness required for toroidal pore formation, and the permanently destabilizing effect of placing even shorter helices into these energy-transducing membranes.

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“…Differences in folding pathways of HKT transporters and their M372del mutants could now be J o u r n a l P r e -p r o o f explored in vitro using cell-free synthesis [56] in a bilayer made of a range of lipids [57][58][59] of allelic variants or truncated and mutated HKTs. It remains to establish if non-functional HvHKT1;5 M372del proteins would maintain stable plasma membrane localisation when expressed in barley using their native promoters, or if membrane proteases would eliminate these functionally unfit proteins to prevent membrane crowding [60].…”

Section: Discussionmentioning

confidence: 99%

A single residue deletion in the barley HKT1;5 P189 variant restores plasma membrane localisation but not Na+ conductance

Wege

Qiu

Byrt

et al. 2021

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Soluble TatA forms oligomers that interact with membranes: Structure and insertion studies of a versatile protein transporter

Cited by 8 publications

References 34 publications

Hydrophobic mismatch is a key factor in protein transport across lipid bilayer membranes via the Tat pathway

Hydrophobic mismatch is a key factor in protein transport across lipid bilayer membranes via the Tat pathway

Hydrophobic mismatch is a key factor in protein transport on the Tat pathway

A single residue deletion in the barley HKT1;5 P189 variant restores plasma membrane localisation but not Na+ conductance

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