Chloroplast nitrite uptake is enhanced in <i>Arabidopsis</i> PII mutants

Ferrario-Méry, Sylvie; Meyer, Christian; Hodges, Michael

doi:10.1016/j.febslet.2008.02.056

Cited by 51 publications

(30 citation statements)

References 31 publications

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“…From these results, a regulatory role of PII in the fine-tuning of fatty acid biosynthesis and partitioning in seeds had been inferred (Baud et al 2010). Furthermore, in A. thaliana PII mutants, nitrite uptake in chloroplast is enhanced (Ferrario-Mery et al 2008), resembling the regulatory defect of nitrite/nitrate uptake in cyanobacterial PII mutants (Kloft and Forchhammer 2005). Altogether, the data indicate that during the evolution of plastids, PII lost its primary function of coordinating gene expression through interactions with PipX, but preserved its role in nitrogen (arginine) storage metabolism, and eventually took over fine-tuned regulation of carbon (fatty acid) storage metabolism.…”

Section: Further Functions Of Pii Signaling In Oxygenic Phototrophsmentioning

confidence: 88%

From cyanobacteria to plants: conservation of PII functions during plastid evolution

Chellamuthu

Alva

Forchhammer

2012

Planta

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This article reviews the current state-of-the-art concerning the functions of the signal processing protein PII in cyanobacteria and plants, with a special focus on evolutionary aspects. We start out with a general introduction to PII proteins, their distribution, and their evolution. We also discuss PII-like proteins and domains, in particular, the similarity between ATP-phosphoribosyltransferase (ATP-PRT) and its PII-like domain and the complex between N-acetyl-L-glutamate kinase (NAGK) and its PII activator protein from oxygenic phototrophs. The structural basis of the function of PII as an ATP/ADP/ 2-oxoglutarate signal processor is described for Synechococcus elongatus PII. In both cyanobacteria and plants, a major target of PII regulation is NAGK, which catalyzes the committed step of arginine biosynthesis. The common principles of NAGK regulation by PII are outlined. Based on the observation that PII proteins from cyanobacteria and plants can functionally replace each other, the hypothesis that PII-dependent NAGK control was under selective pressure during the evolution of plastids of Chloroplastida and Rhodophyta is tested by bioinformatics approaches. It is noteworthy that two lineages of heterokont algae, diatoms and brown algae, also possess NAGK, albeit lacking PII; their NAGK however appears to have descended from an alphaproteobacterium and not from a cyanobacterium as in plants. We end this article by coming to the conclusion that during the evolution of plastids, PII lost its function in coordinating gene expression through the PipX-NtcA network but preserved its role in nitrogen (arginine) storage metabolism, and subsequently took over the fine-tuned regulation of carbon (fatty acid) storage metabolism, which is important in certain developmental stages of plants.

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Section: Further Functions Of Pii Signaling In Oxygenic Phototrophsmentioning

confidence: 88%

From cyanobacteria to plants: conservation of PII functions during plastid evolution

Chellamuthu

Alva

Forchhammer

2012

Planta

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“…Intact rosette leaf chloroplasts were Percoll-purified as described in ref. 24. The plants were maintained in darkness during 24 h to reduce starch levels and minimize chloroplast damage, and were subsequently transferred to light (150 μE·m Expression and Purification of Recombinant Proteins.…”

Section: Methodsmentioning

confidence: 99%

“…The structure of a PII-NAGK complex has been solved for Arabidopsis (22) and Synechococcus elongatus proteins (23). It is possible that the function of plant PII has further similarities to those found in cyanobacteria because it has been proposed that plant PII regu-lates chloroplast nitrite uptake via an interaction with a nitrite transporter (24).…”

mentioning

confidence: 99%

Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate–regulated by interaction of PII with the biotin carboxyl carrier subunit

Feria

Valot

Alain

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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156

142

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The PII protein is a signal integrator involved in the regulation of nitrogen metabolism in bacteria and plants. Upon sensing of cellular carbon and energy availability, PII conveys the signal by interacting with target proteins, thereby modulating their biological activity. Plant PII is located to plastids; therefore, to identify new PII target proteins, PII-affinity chromatography of soluble extracts from Arabidopsis leaf chloroplasts was performed. Several proteins were retained only when Mg-ATP was present in the binding medium and they were specifically released from the resin by application of a 2-oxoglutarate-containing elution buffer. Mass spectroscopy of SDS/PAGE-resolved protein bands identified the biotin carboxyl carrier protein subunits of the plastidial acetyl-CoA carboxylase (ACCase) and three other proteins containing a similar biotin/lipoyl-binding motif as putative PII targets. ACCase is a key enzyme initiating the synthesis of fatty acids in plastids. In in vitro reconstituted assays supplemented with exogenous ATP, recombinant Arabidopsis PII inhibited chloroplastic ACCase activity, and this was completely reversed in the presence of 2-oxoglutarate, pyruvate, or oxaloacetate. The inhibitory effect was PII-dosedependent and appeared to be PII-specific because ACCase activity was not altered in the presence of other tested proteins. PII decreased the V max of the ACCase reaction without altering the K m for acetyl-CoA. These data show that PII function has evolved between bacterial and plant systems to control the carbon metabolism pathway of fatty acid synthesis in plastids.Arabidopsis thaliana | biotin carboxyl carrier protein | PII protein | organic acids | fatty acid metabolism

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“…In higher plants, the PII protein regulates arginine biosynthesis 5 and plays a role in nitrogen regulation. 6 We analyzed the proteins enriched in GO biological process; it was found that the P-II nitrogen sensing protein possessed multifarious functions, such as biological regulation, regulation of biological quality, response to disaccharide stimulus, cellular homeostasis, aromatic compound biosynthetic process, and phenylpropanoid metabolic process (Fig.…”

mentioning

confidence: 99%

“…It has been reported that chloroplast nitrite uptake was enhanced in Arabidopsis PII knockout mutants. 5 The downregulation of P-II nitrogen sensing protein under salt stress probably increase nitrite uptake and nitrogen metabolism. Considering the accumulation of amino acids under stress, 1 the increased P-II nitrogen sensing protein might contribute to synthesis of amino acids, such as proline and non-protein amino acid g-aminobutyric acid (GABA) which play important roles in scavenging ROS and stabilizing the structure of proteins.…”

mentioning

confidence: 99%

Rearrangement of nitrogen metabolism in rice (Oryza sativa L.) under salt stress

Huang

Lan

et al. 2016

Plant Signaling & Behavior

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Chloroplast nitrite uptake is enhanced in Arabidopsis PII mutants

Cited by 51 publications

References 31 publications

From cyanobacteria to plants: conservation of PII functions during plastid evolution

From cyanobacteria to plants: conservation of PII functions during plastid evolution

Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate–regulated by interaction of PII with the biotin carboxyl carrier subunit

Rearrangement of nitrogen metabolism in rice (Oryza sativa L.) under salt stress

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