Chlamydomonas reinhardtii CNX1E Reconstitutes Molybdenum Cofactor Biosynthesis in Escherichia coli Mutants
A Llamas, M Tejada-Jimenez… - Eukaryotic …, 2007 - Am Soc Microbiol
Eukaryotic Cell, 2007•Am Soc Microbiol
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.
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.
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.
American Society for Microbiology