Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts

Negi, Surendra S.; Carol, Andrew A.; Pandya, Shivangi; Braun, Werner; Anderson, Louise E.

doi:10.1016/j.jsb.2007.08.016

Cited by 10 publications

(10 citation statements)

References 33 publications

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“…Modeling the MV F-trimer Structure-The homology model was generated using procedures previously used for other proteins (32)(33)(34). Our modeling package MPACK combines the programs EXDIS (35), DIAMOD (36), and the energy minimization program FANTOM (37).…”

Section: Methodsmentioning

confidence: 99%

Base of the Measles Virus Fusion Trimer Head Receives the Signal That Triggers Membrane Fusion

Apte-Sengupta

Negi

Léonard

et al. 2012

Journal of Biological Chemistry

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Background: A homology model of the trimeric measles virus fusion protein predicts a cavity in the base of the head. Results: Hydrophobic residues required for interactions with the hemagglutinin map to this cavity. Conclusion:The base of the measles virus fusion protein trimer head receives the signal that triggers membrane fusion. Significance: Emerging, re-emerging, and prevalent paramyxoviruses may operate based on similar signal transmission mechanisms.The measles virus (MV) fusion (F) protein trimer executes membrane fusion after receiving a signal elicited by receptor binding to the hemagglutinin (H) tetramer. Where and how this signal is received is understood neither for MV nor for other paramyxoviruses. Because only the prefusion structure of the parainfluenza virus 5 (PIV5) F-trimer is available, to study signal receipt by the MV F-trimer, we generated and energy-refined a homology model. We used two approaches to predict surface residues of the model interacting with other proteins. Both approaches measured interface propensity values for patches of residues. The second approach identified, in addition, individual residues based on the conservation of physical chemical properties among F-proteins. Altogether, about 50 candidate interactive residues were identified. Through iterative cycles of mutagenesis and functional analysis, we characterized six residues that are required specifically for signal transmission; their mutation interferes with fusion, although still allowing efficient F-protein processing and cell surface transport. One residue is located adjacent to the fusion peptide, four line a cavity in the base of the F-trimer head, while the sixth residue is located near this cavity. Hydrophobic interactions in the cavity sustain the fusion process and contacts with H. The cavity is flanked by two different subunits of the F-trimer. Tetrameric H-stalks may be lodged in apposed cavities of two F-trimers. Because these insights are based on a PIV5 homology model, the signal receipt mechanism may be conserved among paramyxoviruses.Measles virus (MV), 2 an enveloped nonsegmented negative strand RNA virus, remains a significant public health problem (1). Although targeted for eradication (2), MV still caused 139,000 worldwide deaths in 2010 (3). In addition, relaxed vaccination discipline favored recent measles re-emergence in Europe and North America, now reporting small but costly epidemics (4, 5).MV is a member of the family Paramyxoviridae that includes other deadly emerging viruses such as Hendra and Nipah and prevalent human pathogens such as mumps, parainfluenza, and respiratory syncytial viruses that still cause significant morbidity and mortality (6). Although many other enveloped viruses take advantage of low pH (7) or proteases (8) in the endosomal compartment to trigger membrane fusion, most paramyxoviruses including MV fuse directly with the plasma membrane (6, 9).An accurate mechanism must be in place to secure timely and efficient MV cell entry at the plasma membrane. It is known tha...

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Section: Methodsmentioning

confidence: 99%

Base of the Measles Virus Fusion Trimer Head Receives the Signal That Triggers Membrane Fusion

Apte-Sengupta

Negi

Léonard

et al. 2012

Journal of Biological Chemistry

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“…FNR is a soluble complex [50], able to bind to ferredoxin on the thylakoid membrane and move through the cytosol. Notably, in pea leaf chloroplasts [51] and diatom plastids [52], FNR binds to glyceraldehyde-3-phosphate dehydrogenase (GAPDH), consistent with NADPH produced by FNR being passed directly to GAPDH. Adding to this idea, the phage gene for CP12, which regulates the Calvin cycle in cyanobacteria [25], was among the most highly expressed phage genes in the light, suggesting that GAPDH in the Calvin cycle is inhibited, consistent with [26].…”

Section: Discussionmentioning

confidence: 99%

Gene Expression Patterns during Light and Dark Infection of Prochlorococcus by Cyanophage

Thompson

Zeng

2016

PLoS ONE

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Cyanophage infecting the marine cyanobacteria Prochlorococcus and Synechococcus require light and host photosystem activity for optimal reproduction. Many cyanophages encode multiple photosynthetic electron transport (PET) proteins, which are presumed to maintain electron flow and produce ATP and NADPH for nucleotide biosynthesis and phage genome replication. However, evidence suggests phage augment NADPH production via the pentose phosphate pathway (PPP), thus calling into question the need for NADPH production by PET. Genes implicated in cyclic PET have since been identified in cyanophage genomes. It remains an open question which mode of PET, cyclic or linear, predominates in infected cyanobacteria, and thus whether the balance is towards producing ATP or NADPH. We sequenced transcriptomes of a cyanophage (P-HM2) and its host (Prochlorococcus MED4) throughout infection in the light or in the dark, and analyzed these data in the context of phage replication and metabolite measurements. Infection was robust in the light, but phage were not produced in the dark. Host gene transcripts encoding high-light inducible proteins and two terminal oxidases (plastoquinol terminal oxidase and cytochrome c oxidase)—implicated in protecting the photosynthetic membrane from light stress—were the most enriched in light but not dark infection. Among the most diminished transcripts in both light and dark infection was ferredoxin–NADP+ reductase (FNR), which uses the electron acceptor NADP+ to generate NADPH in linear photosynthesis. The phage gene for CP12, which putatively inhibits the Calvin cycle enzyme that receives NADPH from FNR, was highly expressed in light infection. Therefore, both PET production of NADPH and its consumption by carbon fixation are putatively repressed during phage infection in light. Transcriptomic evidence is thus consistent with cyclic photophosphorylation using oxygen as the terminal electron acceptor as the dominant mode of PET under infection, with ATP from PET and NADPH from the PPP producing the energy and reducing equivalents for phage nucleotide biosynthesis and replication.

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“…This inhibition was also observed in the desmid Staurastrum cingulum (Maberly et al ., ). In higher plants, immunological studies have shown that many Calvin cycle enzymes, including GAPDH and FNR, are associated with thylakoid membranes (Suss et al ., ; Sainis et al ., ; Negi et al ., ; Agarwal et al ., ). Furthermore, a docking model has shown that it is theoretically possible for GAPDH to form a complex with FNR in Pisum sativum (Negi et al ., ).…”

Section: Discussionmentioning

confidence: 99%

“…In higher plants, immunological studies have shown that many Calvin cycle enzymes, including GAPDH and FNR, are associated with thylakoid membranes (Suss et al, 1993;Sainis et al, 2003;Negi et al, 2008;Agarwal et al, 2009). Furthermore, a docking model has shown that it is theoretically possible for GAPDH to form a complex with FNR in Pisum sativum (Negi et al, 2008). It is therefore possible that this complex is also present elsewhere, but probably with different consequences for regulation.…”

Section: Discussionmentioning

confidence: 99%

“…The activity of the GAPDH-CP12 complex was not affected by addition of BSA, Rubisco (EC 4.1.1.39) or PRK (data not shown). We also tested the effect of the addition of ferredoxin-NADP + reductase (FNR; EC 1.18.1.1) on GAPDH because FNR is inhibited by NADPH (Zanetti & Forti, 1966) and coimmunolocated with GAPDH in pea (Negi et al, 2008). The addition of commercial FNR from S. oleracea inhibited GAPDH activity by 40% under oxidizing conditions when NADPH was present (data not shown), and the effect was abolished by the addition of DTT, in agreement with the patterns observed in Fig.…”

Section: Differential Regulation Of Gapdh Activitymentioning

confidence: 99%

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Glyceraldehyde‐3‐phosphate dehydrogenase is regulated by ferredoxin‐NADP reductase in the diatom Asterionella formosa

et al. 2014

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SummaryDiatoms are a widespread and ecologically important group of heterokont algae that contribute c. 20% to global productivity. Previous work has shown that regulation of their key Calvin cycle enzymes differs from that of the Plantae, and that in crude extracts, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) can be inhibited by nicotinamide adenine dinucleotide phosphate reduced (NADPH) under oxidizing conditions.The freshwater diatom, Asterionella formosa, was studied using enzyme kinetics, chromatography, surface plasmon resonance, mass spectrometry and sequence analysis to determine the mechanism behind this GAPDH inhibition.GAPDH interacted with ferredoxin-nicotinamide adenine dinucleotide phosphate (NADP) reductase (FNR) from the primary phase of photosynthesis, and the small chloroplast protein, CP12. Sequences of copurified GAPDH and FNR were highly homologous with published sequences. However, the widespread ternary complex among GAPDH, phosphoribulokinase and CP12 was absent. Activity measurements under oxidizing conditions showed that NADPH can inhibit GAPDH-CP12 in the presence of FNR, explaining the earlier observed inhibition within crude extracts.Diatom plastids have a distinctive metabolism, including the lack of the oxidative pentose phosphate pathway, and so cannot produce NADPH in the dark. The observed down-regulation of GAPDH in the dark may allow NADPH to be rerouted towards other reductive processes contributing to their ecological success.

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Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts

Cited by 10 publications

References 33 publications

Base of the Measles Virus Fusion Trimer Head Receives the Signal That Triggers Membrane Fusion

Base of the Measles Virus Fusion Trimer Head Receives the Signal That Triggers Membrane Fusion

Gene Expression Patterns during Light and Dark Infection of Prochlorococcus by Cyanophage

Glyceraldehyde‐3‐phosphate dehydrogenase is regulated by ferredoxin‐NADP reductase in the diatom Asterionella formosa

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