Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo

Junling Wang, Xuemei Han, Sougata Saha, Tao Xu, Reena Rai, Fangliang Zhang, Yuri I. Wolf, Alexey Wolfson, John R. Yates, Anna Kashina

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


Posttranslational arginylation mediated by arginyltransferase (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 arginyltransferases 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.

Original languageEnglish (US)
Pages (from-to)121-130
Number of pages10
JournalChemistry and Biology
Issue number1
StatePublished - Jan 28 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry


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