Twin-arginine translocation pathway

Last updated
TatC
Identifiers
SymbolTatC
Pfam PF00902
InterPro IPR002033
TCDB 2.A.64
OPM superfamily 63
OPM protein 4b4a
Membranome 435
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
TatA/B/E
Identifiers
SymbolMttA_Hcf106
Pfam PF02416
InterPro IPR003369
TCDB 2.A.64
OPM superfamily 63
OPM protein 2l16
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The twin-arginine translocation pathway (Tat pathway) is a protein export, or secretion pathway found in plants, bacteria, and archaea. In contrast to the Sec pathway which transports proteins in an unfolded manner, the Tat pathway serves to actively translocate folded proteins across a lipid membrane bilayer. In plants, the Tat translocase is located in the thylakoid membrane of the chloroplast, where it acts to export proteins into the thylakoid lumen. In bacteria, the Tat translocase is found in the cytoplasmic membrane and serves to export proteins to the cell envelope, or to the extracellular space. [1] The existence of a Tat translocase in plant mitochondria is also proposed. [2] [3]

In the plant thylakoid membrane and in Gram-negative bacteria the Tat translocase is composed of three essential membrane proteins; TatA, TatB, and TatC. In the most widely studied Tat pathway, that of the Gram-negative bacterium Escherichia coli , these three proteins are expressed from an operon with a fourth Tat protein, TatD, which is not required for Tat function. A fifth Tat protein TatE that is homologous to the TatA protein is present at a much lower level in the cell than TatA and is not believed to play any significant role in Tat function.

The Tat pathways of Gram-positive bacteria differ in that they do not have a TatB component. In these bacteria the Tat system is made up from a single TatA and TatC component, with the TatA protein being bifunctional and fulfilling the roles of both E. coli TatA and TatB. [4]

The name of the Tat pathway relates to a highly conserved twin-arginine leader motif (S/TRRXFLK) which is found in the N terminal Signal peptide of the corresponding passenger proteins. [5] The signal peptide is removed by a signal peptidase after release of the transported protein from the Tat complex. [6] At least two TatC molecules co-exist within each Tat translocon. [7] [8]

In pathogens

Not all bacteria carry the tatABC genes in their genome; [9] however, of those that do, there seems to be no discrimination between pathogens and nonpathogens. Despite that fact, some pathogenic bacteria such as Pseudomonas aeruginosa , Legionella pneumophila , Yersinia pseudotuberculosis , and E. coli O157:H7 rely on a functioning Tat pathway for full virulence in infection models. In addition, a number of exported virulence factors have been shown to rely on the Tat pathway. One such category of virulence factors are the phospholipase C enzymes, which have been shown to be Tat-exported in Pseudomonas aeruginosa, and thought to be Tat-exported in Mycobacterium tuberculosis .

Related Research Articles

Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, the plasma membrane, or to the exterior of the cell via secretion. Information contained in the protein itself directs this delivery process. Correct sorting is crucial for the cell; errors or dysfunction in sorting have been linked to multiple diseases.

<span class="mw-page-title-main">Thylakoid</span> Membrane enclosed compartments in chloroplasts and cyanobacteria

Thylakoids are membrane-bound compartments inside chloroplasts and cyanobacteria. They are the site of the light-dependent reactions of photosynthesis. Thylakoids consist of a thylakoid membrane surrounding a thylakoid lumen. Chloroplast thylakoids frequently form stacks of disks referred to as grana. Grana are connected by intergranal or stromal thylakoids, which join granum stacks together as a single functional compartment.

<span class="mw-page-title-main">Secretion</span> Controlled release of substances by cells or tissues

Secretion is the movement of material from one point to another, such as a secreted chemical substance from a cell or gland. In contrast, excretion is the removal of certain substances or waste products from a cell or organism. The classical mechanism of cell secretion is via secretory portals at the plasma membrane called porosomes. Porosomes are permanent cup-shaped lipoprotein structures embedded in the cell membrane, where secretory vesicles transiently dock and fuse to release intra-vesicular contents from the cell.

<span class="mw-page-title-main">Elastase</span> Enzyme

In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins. In particular, it is a serine protease.

<i>Pseudomonas aeruginosa</i> Species of bacterium

Pseudomonas aeruginosa is a common encapsulated, gram-negative, aerobic–facultatively anaerobic, rod-shaped bacterium that can cause disease in plants and animals, including humans. A species of considerable medical importance, P. aeruginosa is a multidrug resistant pathogen recognized for its ubiquity, its intrinsically advanced antibiotic resistance mechanisms, and its association with serious illnesses – hospital-acquired infections such as ventilator-associated pneumonia and various sepsis syndromes.

<i>Moraxella catarrhalis</i> Species of bacterium

Moraxella catarrhalis is a fastidious, nonmotile, Gram-negative, aerobic, oxidase-positive diplococcus that can cause infections of the respiratory system, middle ear, eye, central nervous system, and joints of humans. It causes the infection of the host cell by sticking to the host cell using trimeric autotransporter adhesins.

Adhesins are cell-surface components or appendages of bacteria that facilitate adhesion or adherence to other cells or to surfaces, usually in the host they are infecting or living in. Adhesins are a type of virulence factor.

<span class="mw-page-title-main">Bacterial outer membrane</span>

The bacterial outer membrane is found in gram-negative bacteria. Its composition is distinct from that of the inner cytoplasmic cell membrane - among other things, the outer leaflet of the outer membrane of many gram-negative bacteria includes a complex lipopolysaccharide whose lipid portion acts as an endotoxin - and in some bacteria such as E. coli it is linked to the cell's peptidoglycan by Braun's lipoprotein.

<span class="mw-page-title-main">Filamentation</span>

Filamentation is the anomalous growth of certain bacteria, such as Escherichia coli, in which cells continue to elongate but do not divide. The cells that result from elongation without division have multiple chromosomal copies.

Virulence factors are cellular structures, molecules and regulatory systems that enable microbial pathogens to achieve the following:

In molecular biology, the Signal Peptide Peptidase (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs). Its sequences is highly conserved in different vertebrate species. SPP cleaves remnant signal peptides left behind in membrane by the action of signal peptidase and also plays key roles in immune surveillance and the maturation of certain viral proteins.

Translocase is a general term for a protein that assists in moving another molecule, usually across a cell membrane. These enzymes catalyze the movement of ions or molecules across membranes or their separation within membranes. The reaction is designated as a transfer from “side 1” to “side 2” because the designations “in” and “out”, which had previously been used, can be ambiguous. Translocases are the most common secretion system in Gram positive bacteria.

Autoinducers are signaling molecules that are produced in response to changes in cell-population density. As the density of quorum sensing bacterial cells increases so does the concentration of the autoinducer. Detection of signal molecules by bacteria acts as stimulation which leads to altered gene expression once the minimal threshold is reached. Quorum sensing is a phenomenon that allows both Gram-negative and Gram-positive bacteria to sense one another and to regulate a wide variety of physiological activities. Such activities include symbiosis, virulence, motility, antibiotic production, and biofilm formation. Autoinducers come in a number of different forms depending on the species, but the effect that they have is similar in many cases. Autoinducers allow bacteria to communicate both within and between different species. This communication alters gene expression and allows bacteria to mount coordinated responses to their environments, in a manner that is comparable to behavior and signaling in higher organisms. Not surprisingly, it has been suggested that quorum sensing may have been an important evolutionary milestone that ultimately gave rise to multicellular life forms.

<span class="mw-page-title-main">SecY protein</span>

The SecY protein is the main transmembrane subunit of the bacterial Sec export pathway and of a protein-secreting ATPase complex, also known as a SecYEG translocon. Homologs of the SecYEG complex are found in eukaryotes and in archaea, where the subunit is known as Sec61α.

<span class="mw-page-title-main">Trimeric autotransporter adhesin</span> Proteins found on the outer membrane of Gram-negative bacteria

In molecular biology, trimeric autotransporter adhesins (TAAs), are proteins found on the outer membrane of Gram-negative bacteria. Bacteria use TAAs in order to infect their host cells via a process called cell adhesion. TAAs also go by another name, oligomeric coiled-coil adhesins, which is shortened to OCAs. In essence, they are virulence factors, factors that make the bacteria harmful and infective to the host organism.

A target peptide is a short peptide chain that directs the transport of a protein to a specific region in the cell, including the nucleus, mitochondria, endoplasmic reticulum (ER), chloroplast, apoplast, peroxisome and plasma membrane. Some target peptides are cleaved from the protein by signal peptidases after the proteins are transported.

Membrane vesicle trafficking in eukaryotic animal cells involves movement of biochemical signal molecules from synthesis-and-packaging locations in the Golgi body to specific release locations on the inside of the plasma membrane of the secretory cell. It takes place in the form of Golgi membrane-bound micro-sized vesicles, termed membrane vesicles (MVs).

<span class="mw-page-title-main">TIC/TOC complex</span>

The TIC and TOC complexes are translocons located in the chloroplast of a eukaryotic cell, that is, protein complexes that facilitate the transfer of proteins in and out through the chloroplast's membrane. It mainly transports proteins made in the cytoplasm into the chloroplast. The TIC complex(translocon on the inner chloroplast membrane) is located in the inner envelope of the chloroplast. The TOC complex(translocon on the outer chloroplast membrane) is located in the outer envelope of the chloroplast.

<span class="mw-page-title-main">Bacterial secretion system</span> Protein complexes present on the cell membranes of bacteria for secretion of substances

Bacterial secretion systems are protein complexes present on the cell membranes of bacteria for secretion of substances. Specifically, they are the cellular devices used by pathogenic bacteria to secrete their virulence factors to invade the host cells. They can be classified into different types based on their specific structure, composition and activity. Generally, proteins can be secreted through two different processes. One process is a one-step mechanism in which proteins from the cytoplasm of bacteria are transported and delivered directly through the cell membrane into the host cell. Another involves a two-step activity in which the proteins are first transported out of the inner cell membrane, then deposited in the periplasm, and finally through the outer cell membrane into the host cell.

<span class="mw-page-title-main">Pho regulon</span>

The Phosphate (Pho) regulon is a regulatory mechanism used for the conservation and management of inorganic phosphate within the cell. It was first discovered in Escherichia coli as an operating system for the bacterial strain, and was later identified in other species. The Pho system is composed of various components including extracellular enzymes and transporters that are capable of phosphate assimilation in addition to extracting inorganic phosphate from organic sources. This is an essential process since phosphate plays an important role in cellular membranes, genetic expression, and metabolism within the cell. Under low nutrient availability, the Pho regulon helps the cell survive and thrive despite a depletion of phosphate within the environment. When this occurs, phosphate starvation-inducible (psi) genes activate other proteins that aid in the transport of inorganic phosphate.

References

  1. Sargent, F.; Berks, B.C.; Palmer, T. (2006). "Pathfinders and trailblazers: a prokaryotic targeting system for transport of folded proteins". FEMS Microbiol. Lett. 254 (2): 198–207. doi: 10.1111/j.1574-6968.2005.00049.x . PMID   16445746.
  2. Carrie, Chris; Weißenberger, Stefan; Soll, Jürgen (2016-10-15). "Plant mitochondria contain the protein translocase subunits TatB and TatC". Journal of Cell Science. 129 (20): 3935–3947. doi: 10.1242/jcs.190975 . ISSN   0021-9533. PMID   27609835.
  3. Bennewitz, Bationa; Sharma, Mayank; Tannert, Franzisca; Klösgen, Ralf Bernd (November 2020). "Dual targeting of TatA points to a chloroplast-like Tat pathway in plant mitochondria". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1867 (11): 118816. doi: 10.1016/j.bbamcr.2020.118816 . PMID   32768405. S2CID   224889980.
  4. Barnett JP, Eijlander RT, Kuipers OP, Robinson C (2008). "A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes". J. Biol. Chem. 283 (5): 2534–2542. doi: 10.1074/jbc.M708134200 . PMID   18029357.
  5. Chaddock, A.M.; Mant, A.; Karnauchov, I.; Brink, S.; Herrmann, R.G.; Klösgen, R.B.; Robinson, C. (1995). "A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase". EMBO J. 14 (12): 2715–2722. doi:10.1002/j.1460-2075.1995.tb07272.x. PMC   398390 . PMID   7796800.
  6. Frielingsdorf, S.; Klösgen, R.B. (2007). "Prerequisites for Terminal Processing of Thylakoidal Tat Substrates". J. Biol. Chem. 282 (33): 24455–24462. doi: 10.1074/jbc.M702630200 . PMID   17581816.
  7. Sargent F, Bogsch EG, Stanley NR, Wexler M, Robinson C, Berks BC, Palmer T (1998). "Overlapping functions of components of a bacterial Sec-independent protein export pathway". EMBO Journal. 17 (13): 3640–50. doi:10.1093/emboj/17.13.3640. PMC   1170700 . PMID   9649434.
  8. Gouffi K, Santini CL, Wu LF (August 2002). "Topology determination and functional analysis of the Escherichia coli TatC protein". FEBS Lett. 525 (1–3): 65–70. doi:10.1016/s0014-5793(02)03069-7. PMID   12163163.
  9. Organism