Target site specificity and in vivo complexity of the mammalian arginylome
Name
s41598-018-34639-6.pdf
Description
Published version
Size
2.55 MB
Format
Adobe PDF
Checksum (MD5)
fee35386cb43bf71864e82b339196c32
Author(s)
Wang, Junling
Pejaver, Vikas Rao
Dann, Geoffrey P.
Wolf, Maxim Y.
Kellis, Manolis
Huang, Yun
Garcia, Benjamin A.
Radivojac, Predrag
Kashina, Anna
Date Issued
November 2018
Journal
Scientific Reports
Publisher
Springer Science and Business Media LLC
Citation
Wang, Junling et al. "Target site specificity and in vivo complexity of the mammalian arginylome." Scientific Reports 8, 1 (November 2018): 16177 © 2018 The Author(s)
Version
Final published version
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.
MIT Department
Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory
Terms of Use
Creative Commons Attribution 4.0 International license
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1038/s41598-018-34639-6
