ArticleThe Journal of biological chemistry2014
ChlR protein of Synechococcus sp. PCC 7002 is a transcription activator that uses an oxygen-sensitive [4Fe-4S] cluster to control genes involved in pigment biosynthesis.
Article in The Journal of biological chemistry, 2014. 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, 24 citations in OpenAlex.
- From photosynthetic electron flow to gene regulation: redox signal transduction in cyanobacteria.FEMS microbiology reviews · 2026Review
- Carbon Monoxide-Sensing Transcription Factors: Regulators of Microbial Carbon Monoxide Oxidation Pathway Gene Expression.Journal of bacteriology · 2023Review
- Acclimation of the photosynthetic apparatus to low light in a thermophilic Synechococcus sp. strain.Photosynthesis research · 2022Article
- Nitrogen Sources and Iron Availability Affect Pigment Biosynthesis and Nutrient Consumption inMicroorganisms · 2021Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Global Transcriptional Profiling of the CyanobacteriumFrontiers in microbiology · 2019Article
- Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The MarR-like protein PchR (YvmB) regulates expression of genes involved in pulcherriminic acid biosynthesis and in the initiation of sporulation in Bacillus subtilis.BMC microbiology · 2016Article
- The activity of CouR, a MarR family transcriptional regulator, is modulated through a novel molecular mechanism.Nucleic acids research · 2016Article
- Evolutionary Aspects and Regulation of Tetrapyrrole Biosynthesis in Cyanobacteria under Aerobic and Anaerobic Environments.Life (Basel, Switzerland) · 2015Review
- Identification of a Ligand Binding Pocket in LdtR from Liberibacter asiaticus.Frontiers in microbiology · 2015Article
- Fur-type transcriptional repressors and metal homeostasis in the cyanobacterium Synechococcus sp. PCC 7002.Frontiers in microbiology · 2015Article
- A desaturase gene involved in the formation of 1,14-nonadecadiene in Synechococcus sp. strain PCC 7002.Applied and environmental microbiology · 2014Article
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7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Synechococcus sp. PCC 7002 and many other cyanobacteria have two genes that encode key enzymes involved in chlorophyll a, biliverdin, and heme biosynthesis: acsFI/acsFII, ho1/ho2, and hemF/hemN. Under atmospheric O2 levels, AcsFI synthesizes 3,8-divinyl protochlorophyllide from Mg-protoporphyrin IX monomethyl ester, Ho1 oxidatively cleaves heme to form biliverdin, and HemF oxidizes coproporphyrinogen III to protoporphyrinogen IX. Under microoxic conditions, another set of genes directs the synthesis of alternative enzymes AcsFII, Ho2, and HemN. In Synechococcus sp. PCC 7002, open reading frame SynPCC7002_A1993 encodes a MarR family transcriptional regulator, which is located immediately upstream from the operon comprising acsFII, ho2, hemN, and desF (the latter encodes a putative fatty acid desaturase). Deletion and complementation analyses showed that this gene, denoted chlR, is a transcriptional activator that is essential for transcription of the acsFII-ho2-hemN-desF operon under microoxic conditions. Global transcriptome analyses showed that ChlR controls the expression of only these four genes. Co-expression of chlR with a yfp reporter gene under the control of the acsFII promoter from Synechocystis sp. PCC 6803 in Escherichia coli demonstrated that no other cyanobacterium-specific components are required for proper functioning of this regulatory circuit. A combination of analytical methods and Mössbauer and EPR spectroscopies showed that reconstituted, recombinant ChlR forms homodimers that harbor one oxygen-sensitive [4Fe-4S] cluster. We conclude that ChlR is a transcriptional activator that uses a [4Fe-4S] cluster to sense O2 levels and thereby control the expression of the acsFII-ho2-hemN-desF operon.
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