NDLI: Regulation of the Cyanobacterial CO2-Concentrating Mechanism Involves Internal Sensing of NADP+ and α-Ketogutarate Levels by Transcription Factor CcmR

Content Provider	PubMed Central
Author	Daley, Shawn M. E. Kappell, Anthony D. Carrick, Marla J. Burnap, Robert L.
Editor	Bonaventure, Gustavo
Copyright Year	2012
Abstract	Inorganic carbon is the major macronutrient required by organisms utilizing oxygenic photosynthesis for autotrophic growth. Aquatic photoautotrophic organisms are dependent upon a CO2 concentrating mechanism (CCM) to overcome the poor CO2-affinity of the major carbon-fixing enzyme, ribulose-bisphosphate carboxylase/oxygenase (Rubisco). The CCM involves the active transport of inorganic forms of carbon (Ci) into the cell to increase the CO2 concentration around the active site of Rubisco. It employs both bicarbonate transporters and redox-powered CO2-hydration enzymes coupled to membranous NDH-type electron transport complexes that collectively produce Ci concentrations up to a 1000-fold greater in the cytoplasm compared to the external environment. The CCM is regulated: a high affinity CCM comprised of multiple components is induced under limiting external Ci concentrations. The LysR-type transcriptional regulator CcmR has been shown to repress its own expression along with structural genes encoding high affinity Ci transporters distributed throughout the genome of Synechocystis sp. PCC 6803. While much has been learned about the structural genes of the CCM and the identity of the transcriptional regulators controlling their expression, little is known about the physiological signals that elicit the induction of the high affinity CCM. Here CcmR is studied to identify metabolites that modulate its transcriptional repressor activity. Using surface plasmon resonance (SPR) αketoglutarate (α-KG) and the oxidized form of nicotinamide adenine dinucleotide phosphate (NADP+) have been identified as the co-repressors of CcmR. Additionally, ribulose1,5bisphosphate (RuBP) and 2phosphoglycolate (2PG) have been confirmed as co-activators of CmpR which controls the expression of the ABC-type bicarbonate transporter.
Related Links	http://dx.doi.org/10.1371/journal.pone.0041286
Starting Page	41286
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	7
Volume Number	7
Language	English
Publisher	Public Library of Science
Publisher Date	2012-07-20
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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