title: Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.
abstract: Posttranslational arginylation mediated by arginyl transferase (ATE1) plays an important role in cardiovascular development, cell motility, and regulation of cytoskeleton and metabolic enzymes. This protein modification was discovered decades ago, however, the arginylation reaction and the functioning of ATE1 remained poorly understood because of the lack of good biochemical models. Here, we report the development of an in vitro arginylation system, in which ATE1 function and molecular requirements can be tested using purified recombinant ATE1 isoforms supplemented with a controlled number of components. Our results show that arginylation reaction is a self-sufficient, ATP-independent process that can affect different sites in a polypeptide and that arginyl transferases form different molecular complexes in vivo, associate with components of the translation machinery, and have distinct, partially overlapping subsets of substrates, suggesting that these enzymes play different physiological functions.
authors.affiliation: Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
authors.forename: Junling
authors.initials: J
authors.lastname: Wang
authors.forename: Xuemei
authors.initials: X
authors.lastname: Han
authors.forename: Sougata
authors.initials: S
authors.lastname: Saha
authors.forename: Tao
authors.initials: T
authors.lastname: Xu
authors.forename: Reena
authors.initials: R
authors.lastname: Rai
authors.forename: Fangliang
authors.initials: F
authors.lastname: Zhang
authors.forename: Yuri I
authors.initials: YI
authors.lastname: Wolf
authors.forename: Alexey
authors.initials: A
authors.lastname: Wolfson
authors.forename: John R
authors.initials: JR
authors.lastname: Yates
authors.forename: Anna
authors.initials: A
authors.lastname: Kashina
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D019881:Aminoacyltransferases / Q000378:metabolism*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000378:metabolism; D002417:Cattle; D002457:Cell Extracts; D003067:Coenzymes / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism; D051379:Mice; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D002457:Cell Extracts; D003067:Coenzymes; D007527:Isoenzymes; D011506:Proteins; D000255:Adenosine Triphosphate; D019881:Aminoacyltransferases; C019727:arginyltransferase; D001126:Arginine-tRNA Ligase