The Bacterial signal transduction protein <scp>GlnB</scp> regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl‐<scp>CoA</scp> carboxylase

Gerhardt, Edileusa C. M.; Rodrigues, Thiago E.; Müller-Santos, Marcelo; Pedrosa, Fábio O.; Souza, Emanuel Maltempi de; Forchhammer, Karl; Huergo, Luciano F.

doi:10.1111/mmi.12912

Cited by 58 publications

(86 citation statements)

References 47 publications

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“…Disturbance of ACC regulation has been shown to impact the acetyl-CoA pool (Davis et al, 2000; Zha et al, 2009). Recent findings showed that ACC in Arabidopsis thaliana and Escherichia coli is regulated additionally through interaction of BCCP with the P II protein GlnB (Feria Bourrellier et al, 2010; Gerhardt et al, 2015). …”

Section: Introductionmentioning

confidence: 99%

Interaction of the Nitrogen Regulatory Protein GlnB (PII) with Biotin Carboxyl Carrier Protein (BCCP) Controls Acetyl-CoA Levels in the Cyanobacterium Synechocystis sp. PCC 6803

Hauf¹,

Schmid²,

Gerhardt³

et al. 2016

Front. Microbiol.

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The family of PII signal transduction proteins (members GlnB, GlnK, NifI) plays key roles in various cellular processes related to nitrogen metabolism at different functional levels. Recent studies implied that PII proteins may also be involved in the regulation of fatty acid metabolism, since GlnB proteins from Proteobacteria and from Arabidopsis thaliana were shown to interact with biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase (ACC). In case of Escherichia coli ACCase, this interaction reduces the kcat of acetyl-CoA carboxylation, which should have a marked impact on the acetyl-CoA metabolism. In this study we show that the PII protein of a unicellular cyanobacterium inhibits the biosynthetic activity of E. coli ACC and also interacts with cyanobacterial BCCP in an ATP and 2-oxoglutarate dependent manner. In a PII mutant strain of Synechocystis strain PCC 6803, the lacking control leads to reduced acetyl-CoA levels, slightly increased levels of fatty acids and formation of lipid bodies as well as an altered fatty acid composition.

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Section: Introductionmentioning

confidence: 99%

Interaction of the Nitrogen Regulatory Protein GlnB (PII) with Biotin Carboxyl Carrier Protein (BCCP) Controls Acetyl-CoA Levels in the Cyanobacterium Synechocystis sp. PCC 6803

Hauf¹,

Schmid²,

Gerhardt³

et al. 2016

Front. Microbiol.

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“…NrPII proteins are implicated in the regulation of primary carbon metabolism, as well. In land plants and bacteria, a central carbon metabolic enzyme acetyl-CoA carboxylase is directly regulated by nrPIIs 64,65 . In cyanobacteria, nrPIIs are thought to regulate nitrogen assimilation in a carbon-dependent manner 63,66 .…”

Section: Introductionmentioning

confidence: 99%

A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein

Wheatley¹,

Eden

Ngo

et al. 2016

Journal of Molecular Biology

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Autotrophic bacteria rely on various mechanisms to increase intracellular concentrations of inorganic forms of carbon (i.e. bicarbonate and CO2) in order to improve the efficiency with which they can be converted to organic forms. Transmembrane bicarbonate transporters and carboxysomes play key roles in accumulating bicarbonate and carbon dioxide, but other regulatory elements of carbon concentration mechanisms in bacteria are less understood. In this study, after analyzing the genomic regions around α-type carboxysome operons, we characterize a protein that is conserved across these operons but which has not been previously studied. On the basis of a series of apo- and ligand-bound crystal structures and supporting biochemical data, we show that this protein, which we refer to as the carboxysome-associated PII protein (CPII), represents a new and distinct subfamily within the broad superfamily of previously studied PII regulatory proteins, which are generally involved in regulating nitrogen metabolism in bacteria. CPII undergoes dramatic conformational changes in response to ADP binding, and the affinity for nucleotide binding is strongly enhanced by the presence of bicarbonate. CPII therefore appears to be a unique type of PII protein that senses bicarbonate availability, consistent with its apparent genomic association with the carboxysome and its constituents.

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“…More recently, it was also observed that E. coli GlnB can modulate the activity of an enzyme dedicated to the carbon metabolism, i.e., acetyl-CoA carboxylase (ACC) (56).…”

Section: The P II Protein Familymentioning

confidence: 99%

“…3). The BCCP-P II interaction and ACC inhibition are relieved by 2-OG in a dosedependent manner (56). Hence, P II acts as a 2-oxoglutarate-sensitive dissociable regulatory subunit of ACC (Fig.…”

Section: The P II Protein Familymentioning

confidence: 99%

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

Huergo

Dixon

2015

Microbiol Mol Biol Rev

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221

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SUMMARYThe metabolite 2-oxoglutarate (also known as α-ketoglutarate, 2-ketoglutaric acid, or oxoglutaric acid) lies at the intersection between the carbon and nitrogen metabolic pathways. This compound is a key intermediate of one of the most fundamental biochemical pathways in carbon metabolism, the tricarboxylic acid (TCA) cycle. In addition, 2-oxoglutarate also acts as the major carbon skeleton for nitrogen-assimilatory reactions. Experimental data support the conclusion that intracellular levels of 2-oxoglutarate fluctuate according to nitrogen and carbon availability. This review summarizes how nature has capitalized on the ability of 2-oxoglutarate to reflect cellular nutritional status through evolution of a variety of 2-oxoglutarate-sensing regulatory proteins. The number of metabolic pathways known to be regulated by 2-oxoglutarate levels has increased significantly in recent years. The signaling properties of 2-oxoglutarate are highlighted by the fact that this metabolite regulates the synthesis of the well-established master signaling molecule, cyclic AMP (cAMP), inEscherichia coli.

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The Bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl‐CoA carboxylase

Cited by 58 publications

References 47 publications

Interaction of the Nitrogen Regulatory Protein GlnB (PII) with Biotin Carboxyl Carrier Protein (BCCP) Controls Acetyl-CoA Levels in the Cyanobacterium Synechocystis sp. PCC 6803

Interaction of the Nitrogen Regulatory Protein GlnB (PII) with Biotin Carboxyl Carrier Protein (BCCP) Controls Acetyl-CoA Levels in the Cyanobacterium Synechocystis sp. PCC 6803

A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein

The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite

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