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Robertsonian translocation, a chromosomal rearrangement in pairs 13, 14, 15, 21, and 22; Nonreciprocal translocation, transfer of genes from one chromosome to another; PEP group translocation, a method used by bacteria for sugar uptake; Twin-arginine translocation pathway, a protein export pathway found in plants, bacteria, and archaea
EC 7.2.1 Translocation of inorganic cations linked to oxidoreductase reactions; EC 7.2.2 Translocation of inorganic cations linked to the hydrolysis of a nucleoside triphosphate; EC 7.2.4 Translocation of inorganic cations linked to decarboxylation; An important translocase contained in this group is Na+/K+ pump, also known as EC 7.2.2.13.
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.
A previously undescribed proton translocation pathway is formed by six core transmembrane helices. Proton pumping can be initialized by PP(i) hydrolysis, and H + is then transported into the vacuolar lumen through a pathway consisting of Arg 242, Asp 294, Lys 742 and Glu 301.
The translocon (also known as a translocator or translocation channel) is a complex of proteins associated with the translocation of polypeptides across membranes. [1] In eukaryotes the term translocon most commonly refers to the complex that transports nascent polypeptides with a targeting signal sequence into the interior (cisternal or lumenal) space of the endoplasmic reticulum (ER) from ...
The structures of BtuCD and the BtuCD homolog, HI1470/1, represent two different conformational states of an ABC transporter. The predicted translocation pathway in BtuCD is open to the periplasm and closed at the cytoplasmic side of the membrane while that of HI1470/1 faces the opposite direction and open only to the cytoplasm.
ANT has long been thought to function as a homodimer, but this concept was challenged by the projection structure of the yeast Aac3p solved by electron crystallography, which showed that the protein was three-fold symmetric and monomeric, with the translocation pathway for the substrate through the centre. [7]
The translocase of the outer membrane (TOM) forms a complex made of Tom70, Tom22, and Tom20, along with Tom40, Tom7, Tom6, and Tom5.Tom20 and Tom22 are preprotein receptors, which are responsible for recognition of the cleavable presequence possessed by mitochondrial-targeted proteins. [9]