PII Signal Transduction Protein in Chlamydomonas reinhardtii: Localization and Expression Pattern

Ermilova, Elena; Lapina, T. V.; Zalutskaya, Zhanneta; Minaeva, E. V.; Fokina, Oleksandra; Forchhammer, Karl

doi:10.1016/j.protis.2012.04.002

Cited by 28 publications

(53 citation statements)

References 49 publications

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“…Similar expression profiles were found for other regulators as well, for example, NRR1 (Supplemental Figure 18A), a previously identified transcription factor involved in TAG accumulation upon N deprivation (Boyle et al, 2012), and GLB1 (Supplemental Figure 18B), encoding the PII protein, a wellknown regulator of N metabolism in bacteria (Uhrig et al, 2009;Ermilova et al, 2013). We therefore further inspected two transcription factor databases (PlnTFDB [Pérez-Rodríguez et al, 2010] and PlantTFDB 2.0 [Zhang et al, 2011]) for the presence of DNA binding proteins with similar expression patterns to known genes and regulators involved in N assimilation (Supplemental Data Set 13).…”

Section: Candidate Regulatorssupporting

confidence: 71%

Nitrogen-Sparing Mechanisms in Chlamydomonas Affect the Transcriptome, the Proteome, and Photosynthetic Metabolism

et al. 2014

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ORCID IDs: 0000-0002-7487-8014 (S.S.); 0000-0002-2594-509X (S.S.M.)Nitrogen (N) is a key nutrient that limits global primary productivity; hence, N-use efficiency is of compelling interest in agriculture and aquaculture. We used Chlamydomonas reinhardtii as a reference organism for a multicomponent analysis of the N starvation response. In the presence of acetate, respiratory metabolism is prioritized over photosynthesis; consequently, the N-sparing response targets proteins, pigments, and RNAs involved in photosynthesis and chloroplast function over those involved in respiration. Transcripts and proteins of the Calvin-Benson cycle are reduced in N-deficient cells, resulting in the accumulation of cycle metabolic intermediates. Both cytosolic and chloroplast ribosomes are reduced, but via different mechanisms, reflected by rapid changes in abundance of RNAs encoding chloroplast ribosomal proteins but not cytosolic ones. RNAs encoding transporters and enzymes for metabolizing alternative N sources increase in abundance, as is appropriate for the soil environmental niche of C. reinhardtii. Comparison of the N-replete versus N-deplete proteome indicated that abundant proteins with a high N content are reduced in N-starved cells, while the proteins that are increased have lower than average N contents. This sparing mechanism contributes to a lower cellular N/C ratio and suggests an approach for engineering increased N-use efficiency.

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Section: Candidate Regulatorssupporting

confidence: 71%

Nitrogen-Sparing Mechanisms in Chlamydomonas Affect the Transcriptome, the Proteome, and Photosynthetic Metabolism

et al. 2014

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“…However, A. thaliana PII contains N-and C-terminal extensions of 13 and 15 amino acids length, respectively. These extensions are also found in all other plant PII proteins analyzed so far, including green algae, with an exception of chloroplast-encoded PII of red algae (Uhrig et al 2009;Ermilova et al 2012). In the A. thaliana structure, the N-terminal extension is organized opposite to the T-loop, whereas the C-terminal extension folds back towards the effector binding site and in the ATP-free structure, it occupies part of the ATP binding site (Mizuno et al 2007).…”

Section: Pii-like Proteins: Witnesses Of a Widely Distributed Signal mentioning

confidence: 58%

“…Recently, the PII protein from Chlamydomonas reinhardtii was characterized. It has a potentially phosphorylatable threonyl residue at the corresponding position, but like in Arabidopsis, protein phosphorylation analysis revealed only non-phosphorylated PII protein (Ermilova et al 2012). At a first glance, it seems odd that in spite of conservation of this site, phosphorylation of PII seems not to be conserved.…”

Section: Modification Of Pii Proteinsmentioning

confidence: 99%

“…In eukaryotes, PII homologues have only been identified in Chloroplastida (green algae and land plants), where they are nuclear-encoded, and in Rhodophyta, where they are coded by the plastid genome (Uhrig et al 2009). In both these groups, PII is localized in the chloroplast (Hsieh et al 1998;Ermilova et al 2012) and appears to control the key step in arginine synthesis, as in cyanobacteria.…”

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confidence: 99%

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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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“…These observations suggest the recruitment of other components in a signaling pathway, besides protein nitrosylation, to activate the degradation of cytochrome b 6 f complex and biogenesis factors, as is typical in many stress-induced responses. This signaling pathway may include the nitrogen starvation-induced transcription factor NITROGEN RESPONSE REGULATOR1 (Boyle et al, 2012) or the chloroplast ortholog of the PII protein (Hsieh et al, 1998;Ermilova et al, 2013), which in (cyano)-bacteria signals the nitrogen status under antagonistic regulation by a-ketoglutarate (reviewed in Ninfa and Jiang, 2005). It may also involve CYG11, one of the NOresponsive guanylate cyclases that were found in the nuclear genome of C. reinhardtii (de Montaigu et al, 2010), whose expression is increased 20-fold during nitrogen starvation (Sabeeha Merchant, personal communication).…”

Section: Intracellular Nitrite Is the Most Likely Source Of No Producmentioning

confidence: 99%

Nitric Oxide–Triggered Remodeling of Chloroplast Bioenergetics and Thylakoid Proteins upon Nitrogen Starvation inChlamydomonas reinhardtii

et al. 2014

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Starving microalgae for nitrogen sources is commonly used as a biotechnological tool to boost storage of reduced carbon into starch granules or lipid droplets, but the accompanying changes in bioenergetics have been little studied so far. Here, we report that the selective depletion of Rubisco and cytochrome b 6 f complex that occurs when Chlamydomonas reinhardtii is starved for nitrogen in the presence of acetate and under normoxic conditions is accompanied by a marked increase in chlororespiratory enzymes, which converts the photosynthetic thylakoid membrane into an intracellular matrix for oxidative catabolism of reductants. Cytochrome b 6 f subunits and most proteins specifically involved in their biogenesis are selectively degraded, mainly by the FtsH and Clp chloroplast proteases. This regulated degradation pathway does not require light, active photosynthesis, or state transitions but is prevented when respiration is impaired or under phototrophic conditions. We provide genetic and pharmacological evidence that NO production from intracellular nitrite governs this degradation pathway: Addition of a NO scavenger and of two distinct NO producers decrease and increase, respectively, the rate of cytochrome b 6 f degradation; NO-sensitive fluorescence probes, visualized by confocal microscopy, demonstrate that nitrogen-starved cells produce NO only when the cytochrome b 6 f degradation pathway is activated.

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PII Signal Transduction Protein in Chlamydomonas reinhardtii: Localization and Expression Pattern

Cited by 28 publications

References 49 publications

Nitrogen-Sparing Mechanisms in Chlamydomonas Affect the Transcriptome, the Proteome, and Photosynthetic Metabolism

Nitrogen-Sparing Mechanisms in Chlamydomonas Affect the Transcriptome, the Proteome, and Photosynthetic Metabolism

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

Nitric Oxide–Triggered Remodeling of Chloroplast Bioenergetics and Thylakoid Proteins upon Nitrogen Starvation inChlamydomonas reinhardtii

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