Chlamydomonas reinhardtii CNX1E reconstitutes molybdenum cofactor biosynthesis in Escherichia coli mutants

Eukaryot Cell. 2007 Jun;6(6):1063-7. doi: 10.1128/EC.00072-07. Epub 2007 Apr 6.

Abstract

We have isolated and characterized the Chlamydomonas reinhardtii genes for molybdenum cofactor biosynthesis, namely, CNX1G and CNX1E, and expressed them and their chimeric fusions in Chlamydomonas and Escherichia coli. In all cases, the wild-type phenotype was restored in individual mutants as well as in a CNX1G CNX1E double mutant. Therefore, CrCNX1E is the first eukaryotic protein able to complement an E. coli moeA mutant.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algal Proteins / classification
  • Algal Proteins / genetics
  • Algal Proteins / metabolism*
  • Animals
  • Chlamydomonas reinhardtii / genetics
  • Chlamydomonas reinhardtii / metabolism*
  • Coenzymes / biosynthesis*
  • Escherichia coli* / genetics
  • Escherichia coli* / metabolism
  • Genetic Complementation Test
  • Metalloproteins / biosynthesis*
  • Molecular Sequence Data
  • Molybdenum Cofactors
  • Nuclear Proteins / classification
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Phylogeny
  • Protozoan Proteins / classification
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Pteridines
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism

Substances

  • Algal Proteins
  • Coenzymes
  • Metalloproteins
  • Molybdenum Cofactors
  • Nuclear Proteins
  • Protozoan Proteins
  • Pteridines
  • Recombinant Fusion Proteins
  • molybdenum cofactor

Associated data

  • GENBANK/DQ311645
  • GENBANK/DQ311646