ArticleJournal of bacteriology2010
Role for CysJ flavin reductase in molybdenum cofactor-dependent resistance of Escherichia coli to 6-N-hydroxylaminopurine.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 28 citations in OpenAlex.
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- Transposon Insertion in thePathogens (Basel, Switzerland) · 2020Article
- Comment on "A commensal strain ofScience advances · 2019Article
- From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC.Molecules (Basel, Switzerland) · 2018Review
- Crystal structure of the hydroxylaminopurine resistance protein, YiiM, and its putative molybdenum cofactor-binding catalytic site.Scientific reports · 2018Article
- A commensal strain ofScience advances · 2018Article
- Study of Different Variants of Mo Enzyme crARC and the Interaction with Its Partners crCytb5-R and crCytb5-1.International journal of molecular sciences · 2017Article
- Beyond Tryptophan Synthase: Identification of Genes That Contribute to Chlamydia trachomatis Survival during Gamma Interferon-Induced Persistence and Reactivation.Infection and immunity · 2016Article
- The mammalian molybdenum enzymes of mARC.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
- TusA (YhhP) and IscS are required for molybdenum cofactor-dependent base-analog detoxification.MicrobiologyOpen · 2013Article
- The Chlamydomonas reinhardtii molybdenum cofactor enzyme crARC has a Zn-dependent activity and protein partners similar to those of its human homologue.Eukaryotic cell · 2011Article
- The twists and turns of enzyme function.Journal of bacteriology · 2010Article
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3 authors at 1 institution in 1 country.
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Abstract
We have previously described a novel Escherichia coli detoxification system for the removal of toxic and mutagenic N-hydroxylated nucleobases and related compounds that requires the molybdenum cofactor. Two subpathways (ycbX and yiiM) were identified, each employing a novel molybdo activity capable of inactivating N-hydroxylated compounds by reduction to the corresponding amine. In the present study, we identify the cysJ gene product as one additional component of this system. While the CysJ protein has been identified as the NADPH:flavin oxidoreductase component of the CysJI sulfite reductase complex (CysJ(8)I(4)), we show that the role of CysJ in base analog detoxification is unique and independent of CysI and sulfite reductase. We further show that CysJ functions as a specific partner of the YcbX molybdoenzyme. We postulate that the function of CysJ in this pathway is to provide, via its NADPH:flavin reductase activity, the reducing equivalents needed for the detoxification reaction at the YcbX molybdocenter. In support of the proposed interaction of the CysJ and YcbX proteins, we show that an apparent CysJ-YcbX "hybrid" protein from two Vibrio species is capable of compensating for a double cysJ ycbX defect in E. coli.
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