High-Throughput Identification of Catalytic Redox-Active Cysteine Residues

Authors

Dmitri E. Fomenko, University of Nebraska-LincolnFollow
Weibing Xing, University of North Carolina, Chapel Hill, NC
Blakely M. Adair, U.S. Environmental Protection Agency
David J. Thomas, U.S. Environmental Protection Agency
Vadim Gladyshev, University of Nebraska-LincolnFollow

Date of this Version

January 2007

Comments

Published in SCIENCE - VOL 315 - 19 JANUARY 2007. Copyright 2007. Permission to use. www.sciencemag.org.

Abstract

Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases. This method is independent of protein family, structure, and taxon. We used it to selectively detect the majority of known proteins with redoxactive Cys and to make additional predictions, one of which was verified. Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins.