Possible involvement of cyclic adenosine 3',5'-monophosphate in the regulation of NADP-/NAD-glutamate dehydrogenase ratio and in yeast-mycelium transition of Benjaminiella poitrasii

Khale-Kumar, Ameeta; Deshpande, Mukund V.

doi:10.1128/jb.175.18.6052-6055.1993

Cited by 11 publications

(4 citation statements)

References 17 publications

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“…The relative proportion of active NAD- and NADP-GDH enzymes was reported as biochemical correlate of Y-H dimorphism in B . poitrasii [ 10 , 11 ]. Now in the light of identified reference genes, Ubc and WS-21 , it would be useful to know the transcriptional changes in biochemical correlates during Y-H dimorphism in B .…”

Section: Discussionmentioning

confidence: 99%

Selection of reference genes for quantitative real-time RT-PCR assays in different morphological forms of dimorphic zygomycetous fungus Benjaminiella poitrasii

2017

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Benjaminiella poitrasii, a dimorphic non-pathogenic zygomycetous fungus, exhibits a morphological yeast (Y) to hypha (H) reversible transition in the vegetative phase, sporangiospores (S) in the asexual phase and zygospores (Z) in the sexual phase. To study the gene expression across these diverse morphological forms, suitable reference genes are required. In the present study, 13 genes viz. ACT, 18S rRNA, eEF1α, eEF-Tu,eIF-1A, Tub-α, Tub-b, Ubc, GAPDH, Try, WS-21, NADGDH and NADPGDH were evaluated for their potential as a reference, particularly for studying gene expression during the Y-H reversible transition and also for other asexual and sexual life stages of B. poitrasii. Analysis of RT-qPCR data using geNorm, normFinder and BestKeeper software revealed that genes such as Ubc, 18S rRNA and WS-21 were expressed at constant levels in each given subset of RNA samples from all the morphological phases of B. poitrasii. Therefore, these reference genes can be used to elucidate the role of morpho-genes in B. poitrasii. Further, use of the two most stably expressed genes (Ubc and WS-21) to normalize the expression of the ornithine decarboxylase gene (Bpodc) in different morphological forms of B. poitrasii, generated more reliable results, indicating that our selection of reference genes was appropriate.

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Section: Discussionmentioning

confidence: 99%

Selection of reference genes for quantitative real-time RT-PCR assays in different morphological forms of dimorphic zygomycetous fungus Benjaminiella poitrasii

2017

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“…Another metabolic enzyme and a putative substrate of calcineurin identified in this study is NADP + -dependent glutamate dehydrogenase (NADP-GDH). Interestingly, the levels and phosphorylation state of NADP-GDH are associated with the dimorphic transition between yeast and hyphae in fungi [40] , [41] . Calcineurin-controlled morphogenic transitions have been documented in major human and plant fungal pathogens including C. neoformans , Aspergillus fumigatus , Magnaporthe oryzae , and Ustilago maydis (recently reviewed in [42] ).…”

Section: Discussionmentioning

confidence: 99%

Association of Calcineurin with the COPI Protein Sec28 and the COPII Protein Sec13 Revealed by Quantitative Proteomics

et al. 2011

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Calcineurin is a calcium-calmodulin-dependent serine/threonine specific protein phosphatase operating in key cellular processes governing responses to extracellular cues. Calcineurin is essential for growth at high temperature and virulence of the human fungal pathogen Cryptococcus neoformans but the underlying mechanism is unknown. We performed a mass spectrometry analysis to identify proteins that associate with the calcineurin A catalytic subunit (Cna1) in C. neoformans cells grown under non-stress and high temperature stress conditions. A novel prioritization strategy for mass spectrometry data from immunoprecipitation experiments identified putative substrates and proteins potentially operating with calcineurin in common pathways. Cna1 co-purified with proteins involved in membrane trafficking including the COPI component Sec28 and the COPII component Sec13. The association of Cna1 with Sec28 and Sec13 was confirmed by co-immunoprecipitation. Cna1 exhibited a dramatic change in subcellular localization during high temperature stress from diffuse cytoplasmic to ER-associated puncta and the mother-bud neck and co-localized with Sec28 and Sec13.

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“…Reactivation via dephosphorylation is catalyzed by protein phosphatases. In contrast, phosphorylation of NADP + -specific GDH in the lower fungi Benjaminiella poitrasii was shown to activate the enzyme [130,131]. Differences in the GDH phosphorylation level were shown under nitrogen starvation (NAD + -specific GDH in C. utilis and S. cerevisiae ) or in yeast and mycelium states (NADP + -specific GDH in B. poitrasii) .…”

Section: Post-translational Modifications Of Gdh and Their Biologimentioning

confidence: 99%

“…Differences in the GDH phosphorylation level were shown under nitrogen starvation (NAD + -specific GDH in C. utilis and S. cerevisiae ) or in yeast and mycelium states (NADP + -specific GDH in B. poitrasii) . The findings suggested that phosphorylation of fungal GDH affects the ratio between the different GDH activities, which is important for metabolic regulation [92,131]. …”

Section: Post-translational Modifications Of Gdh and Their Biologimentioning

confidence: 99%

Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications

Bunik

Artiukhov

Aleshin

et al. 2016

Biology

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Glutamate dehydrogenase (GDH) of animal cells is usually considered to be a mitochondrial enzyme. However, this enzyme has recently been reported to be also present in nucleus, endoplasmic reticulum and lysosomes. These extramitochondrial localizations are associated with moonlighting functions of GDH, which include acting as a serine protease or an ATP-dependent tubulin-binding protein. Here, we review the published data on kinetics and localization of multiple forms of animal GDH taking into account the splice variants, post-translational modifications and GDH isoenzymes, found in humans and apes. The kinetic properties of human GLUD1 and GLUD2 isoenzymes are shown to be similar to those published for GDH1 and GDH2 from bovine brain. Increased functional diversity and specific regulation of GDH isoforms due to alternative splicing and post-translational modifications are also considered. In particular, these structural differences may affect the well-known regulation of GDH by nucleotides which is related to recent identification of thiamine derivatives as novel GDH modulators. The thiamine-dependent regulation of GDH is in good agreement with the fact that the non-coenzyme forms of thiamine, i.e., thiamine triphosphate and its adenylated form are generated in response to amino acid and carbon starvation.

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Possible involvement of cyclic adenosine 3',5'-monophosphate in the regulation of NADP-/NAD-glutamate dehydrogenase ratio and in yeast-mycelium transition of Benjaminiella poitrasii

Cited by 11 publications

References 17 publications

Selection of reference genes for quantitative real-time RT-PCR assays in different morphological forms of dimorphic zygomycetous fungus Benjaminiella poitrasii

Selection of reference genes for quantitative real-time RT-PCR assays in different morphological forms of dimorphic zygomycetous fungus Benjaminiella poitrasii

Association of Calcineurin with the COPI Protein Sec28 and the COPII Protein Sec13 Revealed by Quantitative Proteomics

Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications

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