Chlamydomonas reinhardtii CNX1E Reconstitutes Molybdenum Cofactor Biosynthesis in Escherichia coli Mutants
Author(s) -
Ángel Llamas,
Manuel TejadaJiménez,
David González-Ballester,
José Javier Higuera,
Günter Schwarz,
Aurora Galván,
Emilio Muñoz Fernández
Publication year - 2007
Publication title -
eukaryotic cell
Language(s) - English
Resource type - Journals
eISSN - 1535-9778
pISSN - 1535-9786
DOI - 10.1128/ec.00072-07
Subject(s) - chlamydomonas reinhardtii , biosynthesis , mutant , escherichia coli , molybdenum cofactor , biology , cofactor , chlamydomonas , molybdenum , biochemistry , chemistry , gene , enzyme , inorganic chemistry
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.
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