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Chapter 5 : The Twin-Arginine Pathway for Protein Secretion

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Abstract:

About 20 to 30% of proteins synthesized in the bacterial cytoplasm are destined for extracytoplasmic locations ( ). They pass the cytoplasmic membrane using specialized transport systems, involving gated pores, energy, and signal peptides to direct protein export. Two major protein export systems are known, namely, the general retory (Sec) pathway and the win-rginine ranslocation (Tat) pathway ( Fig. 1 ). Most proteins use the Sec pathway, common to all domains of life. The Tat pathway, the focus of this review, is more exclusive. For example, it has only ∼30 native substrates in the Gram-negative bacterium , and it is not universally conserved ( ).

Citation: Frain K, van Dijl J, Robinson C. 2019. The Twin-Arginine Pathway for Protein Secretion, p 53-66. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/ecosalplus.ESP-0040-2018
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Figure 1

Proteins always originate from translating ribosomes (R). Their N-terminal signal peptide (OmpA or TorA in this overview) directs the nascent polypeptide chain to the correct translocase (Sec or Tat, respectively), which may be aided by chaperones. The unfolded Sec protein is transferred to SecA, where it is threaded through the SecYEG channel in the plasma membrane, powered by repeated cycles of ATP binding and hydrolysis. In the oxidizing periplasm, the unfolded protein assumes its tertiary fully folded state. The Tat-dependently translocated protein is fully folded within the cytoplasm, where it may also acquire its cofactor. Once directed to TatBC, TatA protomers are recruited to translocate the protein across the cytoplasmic membrane. Energy required for this process is created by the PMF. mRNA molecules are schematically represented by an interrupted line, synthesized proteins by uninterrupted lines, and translocase subunits by cylinders.

Citation: Frain K, van Dijl J, Robinson C. 2019. The Twin-Arginine Pathway for Protein Secretion, p 53-66. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/ecosalplus.ESP-0040-2018
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Image of Figure 2
Figure 2

The structure of Tat and Sec signal peptides includes three regions, namely, a basic N domain, a hydrophobic H domain, and a polar C domain. A signal peptidase cleavage site (AxA) is positioned prior to the mature protein. The amino acid sequences of the TorA and OmpA signal peptides are specified. Tat signal peptides (top) have a consensus motif containing twin arginines, while Sec signal peptides do not contain this motif. Sec signal peptides tend to be shorter, with fewer residues in their N and H domains, than Tat signal peptides.

Citation: Frain K, van Dijl J, Robinson C. 2019. The Twin-Arginine Pathway for Protein Secretion, p 53-66. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/ecosalplus.ESP-0040-2018
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Figure 3

Three essential components form the Gram-negative bacterial Tat complex, namely, TatA, TatB, and TatC. TatA/E and TatB have similar topologies in that they have one TM helix domain with a short periplasmic N-terminal region, a tilted APH, and an unstructured C terminus on the cytoplasmic side of the plasma membrane. Notably, TatB is larger than TatA, with a longer C-terminal tail. TatC is significantly bigger, as it contains 6 membrane-embedded helices with both the C- and N-terminal ends residing in the cytoplasm. Helices 5 and 6 do not fully span the membrane, which may contribute to TatC’s function.

Citation: Frain K, van Dijl J, Robinson C. 2019. The Twin-Arginine Pathway for Protein Secretion, p 53-66. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/ecosalplus.ESP-0040-2018
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Tables

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Table 1

Molecular masses of Tat proteins and complexes in and

Citation: Frain K, van Dijl J, Robinson C. 2019. The Twin-Arginine Pathway for Protein Secretion, p 53-66. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/ecosalplus.ESP-0040-2018

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