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PMID: 19181668 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.

The Journal of biological chemistry ·Vol. 284 ·No. 15 ·2009-04-10 ·Pages 10150-9

Ren G, Stephan D, Xu Z, Zheng Y, Tang D, Harrison RS, Kurz M, Jarrott R, Shouldice SR, Hiniker A, Martin JL, Heras B, Bardwell JC

Abstract

The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.

MeSH Terms
Amino Acid Sequence Escherichia coli/metabolism Escherichia coli Proteins/chemistry,metabolism Hydrogen-Ion Concentration Isoleucine/chemistry Kinetics Molecular Conformation Molecular Sequence Data Oxidation-Reduction Oxidoreductases/chemistry Proline/chemistry Protein Conformation Protein Disulfide-Isomerases/chemistry,metabolism Protein Folding Protein Structure, Secondary Thioredoxins/chemistry
Chemicals
Escherichia coli Proteins Isoleucine Thioredoxins Proline Oxidoreductases Protein Disulfide-Isomerases dsbA protein, E coli
Authors & Affiliations
13 authors, click to expand affiliations / ORCID
Ren Guoping
Howard Hughes Medical Institute, Departments of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
Stephan Daniel
Xu Zhaohui
Zheng Ying
Tang Danming
Harrison Rosemary S
Kurz Mareike
Jarrott Russell
Shouldice Stephen R
Hiniker Annie
Martin Jennifer L
Heras Begoña
Bardwell James C A
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Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
DOI
10.1074/jbc.M809509200
Published
2009-04-10
Epub
2009-00-30
Pages
10150-9
Language
English
Region
United States
NLM ID
2985121R
PMCID
PMC2665069
Subset
IM
External Links
PubMed source DOI: 10.1074/jbc.M809509200 PMC Full Text View journal details
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