Target site specificity and in vivo complexity of the mammalian arginylome. Academic Article uri icon

Overview

abstract

  • Protein arginylation mediated by arginyltransferase ATE1 is a key regulatory process essential for mammalian embryogenesis, cell migration, and protein regulation. Despite decades of studies, very little is known about the specificity of ATE1-mediated target site recognition. Here, we used in vitro assays and computational analysis to dissect target site specificity of mouse arginyltransferases and gain insights into the complexity of the mammalian arginylome. We found that the four ATE1 isoforms have different, only partially overlapping target site specificity that includes more variability in the target residues than previously believed. Based on all the available data, we generated an algorithm for identifying potential arginylation consensus motif and used this algorithm for global prediction of proteins arginylated in vivo on the N-terminal D and E. Our analysis reveals multiple proteins with potential ATE1 target sites and expand our understanding of the biological complexity of the intracellular arginylome.

publication date

  • November 1, 2018

Research

keywords

  • Aminoacyltransferases
  • Arginine
  • Computational Biology

Identity

PubMed Central ID

  • PMC6212499

Scopus Document Identifier

  • 85055916747

Digital Object Identifier (DOI)

  • 10.1093/bioinformatics/btr209

PubMed ID

  • 30385798

Additional Document Info

volume

  • 8

issue

  • 1