Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin

Martijn A. Huynen, Chris A.E.M. Spronk, Toni Gabaldón, Berend Snel

Research output: Contribution to journalArticleAcademicpeer-review


Genomes, functional genomics data and 3D structure reflect different aspects of protein function. Here, we combine these data to predict that BolA, a widely distributed protein family with unknown function, is a reductase that interacts with a glutaredoxin. Comparisons at the 3D structure level as well as at the sequence profile level indicate homology between BolA and OsmC, an enzyme that reduces organic peroxides. Complementary to this, comparative analyses of genomes and genomics data provide strong evidence of an interaction between BolA and the mono-thiol glutaredoxin family. The interaction between BolA and a mono-thiol glutaredoxin is of particular interest because BolA does not, in contrast to its homolog OsmC, have evolutionarily conserved cysteines to provide it with reducing equivalents. We propose that BolA uses the mono-thiol glutaredoxin as the source for these. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)591-596
Number of pages6
JournalFEBS Letters
Issue number3
Publication statusPublished - 31 Jan 2005


  • BolA
  • Comparative genomics
  • Mono-thiol glutaredoxin
  • Protein function prediction
  • Uvi31+
  • glutaredoxin
  • oxidoreductase
  • article
  • genome
  • genomics
  • molecular evolution
  • priority journal
  • protein function
  • protein protein interaction
  • reduction
  • sequence homology


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