Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published July 5, 2002 | Supplemental Material
Journal Article Open

An Essential Role of N-Terminal Arginylation in Cardiovascular Development


The enzymatic conjugation of arginine to the N-termini of proteins is a part of the ubiquitin-dependent N-end rule pathway of protein degradation. In mammals, three N-terminal residues—aspartate, glutamate, and cysteine—are substrates for arginylation. The mouseATE1 gene encodes a family of Arg-tRNA-protein transferases (R-transferases) that mediate N-terminal arginylation. We constructed ATE1-lacking mouse strains and found thatATE1 −/− embryos die with defects in heart development and in angiogenic remodeling of the early vascular plexus. Through biochemical analyses, we show that N-terminal cysteine, in contrast to N-terminal aspartate and glutamate, is oxidized before its arginylation by R-transferase, suggesting that the arginylation branch of the N-end rule pathway functions as an oxygen sensor.

Additional Information

© 2002 American Association for the Advancement of Science. 3 January 2002; Accepted 5 June 2002. We thank D. Anderson, D. Shin, and Y. Mukouyama for helpful discussions; C. Brower for comments on the manuscript; S. Pease, B. Kennedy, and L. Sandoval for expert care of mice; G. Hathaway for sequencing of RGS4; N. Dinh and M. Young for mass spectrometry; and J. K. Yoon for pLacF. Supported by NIH grant GM31530 and a Kirsch Foundation grant to A.V.

Attached Files

Supplemental Material - KwonSOM.pdf


Files (237.3 kB)
Name Size Download all
237.3 kB Preview Download

Additional details

August 19, 2023
October 18, 2023