气候变化领域集成服务门户(CCPortal): The novel PII-interactor PirC identifies phosphoglycerate mutase as key control point of carbon storage metabolism in cyanobacteria

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DOI	10.1073/pnas.2019988118
	The novel PII-interactor PirC identifies phosphoglycerate mutase as key control point of carbon storage metabolism in cyanobacteria
	Orthwein T.; Scholl J.; Spät P.; Lucius S.; Koch M.; Macek B.; Hagemann M.; Forchhammer K.
发表日期	2021
ISSN	00278424
卷号	118 期号:6
英文摘要	Nitrogen limitation imposes a major transition in the lifestyle of nondiazotrophic cyanobacteria that is controlled by a complex interplay of regulatory factors involving the pervasive signal processor PII. Immediately upon nitrogen limitation, newly fixed carbon is redirected toward glycogen synthesis. How the metabolic switch for diverting fixed carbon toward the synthesis of glycogen or of cellular building blocks is operated was so far poorly understood. Here, using the nondiazotrophic cyanobacterium Synechocystis sp. PCC 6803 as model system, we identified a novel PII interactor, the product of the sll0944 gene, which we named PirC. We show that PirC binds to and inhibits the activity of 2,3-phosphoglycerate-independent phosphoglycerate mutase (PGAM), the enzyme that deviates newly fixed CO2 toward lower glycolysis. The binding of PirC to either PII or PGAM is tuned by the metabolite 2-oxoglutarate (2-OG), which accumulates upon nitrogen starvation. In these conditions, the high levels of 2-OG dissociate the PirC-PII complex to promote PirC binding to and inhibition of PGAM. Accordingly, a PirC-deficient mutant showed strongly reduced glycogen levels upon nitrogen deprivation, whereas polyhydroxybutyrate granules were overaccumulated compared to wild-type. Metabolome analysis revealed an imbalance in 3-phosphoglycerate to pyruvate levels in the pirC mutant, confirming that PirC controls the carbon flux in cyanobacteria via mutually exclusive interaction with either PII or PGAM. © This open access article is distributed under Creative Commons Attribution-NonCommercialNoDerivatives License 4.0 (CC BY-NC-ND).
英文关键词	Carbon flow; Cyanobacteria; Glycogen metabolism; Nitrogen starvation; Polyhydroxybutyrate
语种	英语
scopus关键词	2 oxoglutaric acid; bacterial protein; carbon dioxide; phosphoglycerate mutase; protein PII; protein PirC; pyruvic acid; unclassified drug; Article; bacterial gene; bioaccumulation; carbon metabolism; carbon storage; controlled study; enzyme activity; enzyme inhibition; enzyme kinetics; glycolysis; metabolome; nitrogen metabolism; nonhuman; priority journal; protein analysis; protein binding; protein function; protein protein interaction; signal transduction; sll0944 gene; Synechocystis
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180749
作者单位	Interfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, Tübingen, 72076, Germany; Department of Quantitative Proteomics, University of Tübingen, Tübingen, 72076, Germany; Institute of Biological Sciences, Plant Physiology Department, University of Rostock, Rostock, 18059, Germany
推荐引用方式 GB/T 7714	Orthwein T.,Scholl J.,Spät P.,et al. The novel PII-interactor PirC identifies phosphoglycerate mutase as key control point of carbon storage metabolism in cyanobacteria[J],2021,118(6).
APA	Orthwein T..,Scholl J..,Spät P..,Lucius S..,Koch M..,...&Forchhammer K..(2021).The novel PII-interactor PirC identifies phosphoglycerate mutase as key control point of carbon storage metabolism in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America,118(6).
MLA	Orthwein T.,et al."The novel PII-interactor PirC identifies phosphoglycerate mutase as key control point of carbon storage metabolism in cyanobacteria".Proceedings of the National Academy of Sciences of the United States of America 118.6(2021).