NtcA is responsible for accumulation of the small isoform of ferredoxin:NADP oxidoreductase

Omairi-Nasser, Amin; Galmozzi, Carla V.; Latifi, Amel; Muro‐Pastor, M. Isabel; Ajlani, Ghada

doi:10.1099/mic.0.076042-0

Cited by 13 publications

(7 citation statements)

References 22 publications

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“…Further, NtcA activates transcription of the petH promoter in Synechocystis sp. PCC 6803 (78). This suggests that NtcA plays an important role in coordinating the activities of the N assimilation and photosynthesis processes by currently unknown mechanisms.…”

Section: Resultsmentioning

confidence: 99%

Quantitative Proteomics Shows Extensive Remodeling Induced by Nitrogen Limitation in Prochlorococcus marinus SS120

et al. 2017

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Prochlorococcus is the most abundant photosynthetic organism on Earth, contributing significantly to global primary production and playing a prominent role in biogeochemical cycles. Here we study the effects of extreme nitrogen limitation, a feature of the oligotrophic oceans inhabited by this organism. Quantitative proteomics allowed an accurate quantification of the Prochlorococcus proteome, finding three main responses to nitrogen limitation: upregulation of nitrogen assimilation-related proteins, including transporters; downregulation of ribosome proteins; and induction of the photosystem II cyclic electron flow. This suggests that nitrogen limitation affects a range of metabolic processes far wider than initially believed, with the ultimate goal of saving nitrogen and maximizing the nitrogen uptake and assimilation capabilities of the cell.

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Section: Resultsmentioning

confidence: 99%

Quantitative Proteomics Shows Extensive Remodeling Induced by Nitrogen Limitation in Prochlorococcus marinus SS120

et al. 2017

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“…Current knowledge of heterocyst-specific metabolism does not allow us to make a direct distinction between possible electron donors to Flv3B. Nevertheless, it is known that heterocysts harbor only the "short" form of ferredoxin:NADPH oxidoreductase (FNR), i.e., the form that lacks the PBS-binding domain and is active in oxidation of NADPH, making it unlikely that NADP + is reduced on the reducing side of PS I in heterocysts (28). Therefore, it is conceivable that both NADPH and NADH are produced by glycolysis and oxidative pentose phosphate pathway (OPPP) equally in darkness and under the light.…”

Section: Discussionmentioning

confidence: 99%

Heterocyst-specific flavodiiron protein Flv3B enables oxic diazotrophic growth of the filamentous cyanobacterium Anabaena sp. PCC 7120

Ermakova

Battchikova

Richaud

et al. 2014

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

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Flavodiiron proteins are known to have crucial and specific roles in photoprotection of photosystems I and II in cyanobacteria. The filamentous, heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120 contains, besides the four flavodiiron proteins Flv1A, Flv2, Flv3A, and Flv4 present in vegetative cells, two heterocyst-specific flavodiiron proteins, Flv1B and Flv3B. Here, we demonstrate that Flv3B is responsible for light-induced O 2 uptake in heterocysts, and that the absence of the Flv3B protein severely compromises the growth of filaments in oxic, but not in microoxic, conditions. It is further demonstrated that Flv3B-mediated photosynthetic O 2 uptake has a distinct role in heterocysts which cannot be substituted by respiratory O 2 uptake in the protection of nitrogenase from oxidative damage and, thus, in an efficient provision of nitrogen to filaments. In line with this conclusion, the Δflv3B strain has reduced amounts of nitrogenase NifHDK subunits and shows multiple symptoms of nitrogen deficiency in the filaments. The apparent imbalance of cytosolic redox state in Δflv3B heterocysts also has a pronounced influence on the amounts of different transcripts and proteins. Therefore, an O 2 -related mechanism for control of gene expression is suggested to take place in heterocysts.nitrogen fixation | oxygen protection | photosynthesis

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“…In the transcript with a shorter 5′ UTR, initiated at the promoter more proximal to the primary start codon of the gene, the pTIS becomes accessible and FNR L is preferentially synthesized. Similar mechanisms are used for controlled utilization of alternative initiation sites in the petH genes in a range of cyanobacteria (106). This elegant regulatory scheme illustrates how mRNA conformations enable ribosomes to choose between different TISs.…”

Section: The Function Of the Alternative Protein Differs Significantlmentioning

confidence: 85%

Genes within Genes in Bacterial Genomes

2018

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Genetic coding in bacteria largely operates via the "one gene-one protein" paradigm. However, the peculiarities of the mRNA structure, the versatility of the genetic code, and the dynamic nature of translation sometimes allow organisms to deviate from the standard rules of protein encoding. Bacteria can use several unorthodox modes of translation to express more than one protein from a single mRNA cistron. One such alternative path is the use of additional translation initiation sites within the gene. Proteins whose translation is initiated at different start sites within the same reading frame will differ in their N termini but will have identical C-terminal segments. On the other hand, alternative initiation of translation in a register different from the frame dictated by the primary start codon will yield a protein whose sequence is entirely different from the one encoded in the main frame. The use of internal mRNA codons as translation start sites is controlled by the nucleotide sequence and the mRNA folding. The proteins of the alternative proteome generated via the "genes-within-genes" strategy may carry important functions. In this review, we summarize the currently known examples of bacterial genes encoding more than one protein due to the utilization of additional translation start sites and discuss the known or proposed functions of the alternative polypeptides in relation to the main protein product of the gene. We also discuss recent proteome- and genome-wide approaches that will allow the discovery of novel translation initiation sites in a systematic fashion.

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NtcA is responsible for accumulation of the small isoform of ferredoxin:NADP oxidoreductase

Cited by 13 publications

References 22 publications

Quantitative Proteomics Shows Extensive Remodeling Induced by Nitrogen Limitation in Prochlorococcus marinus SS120

Quantitative Proteomics Shows Extensive Remodeling Induced by Nitrogen Limitation in Prochlorococcus marinus SS120

Heterocyst-specific flavodiiron protein Flv3B enables oxic diazotrophic growth of the filamentous cyanobacterium Anabaena sp. PCC 7120

Genes within Genes in Bacterial Genomes

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