02016nas a2200277 4500008004100000022001400041245011600055210006900171260009900240300001400339490000800353520100300361653002801364653001501392653001701407653003201424100001801456700002201474700001401496700001701510700001601527700002101543700002101564700002601585856012701611 2010 eng d a0960-852400aFlocculation of dimorphic yeast benjaminiella poitrasii is altered by modulation of NAD-glutamate dehydrogenase0 aFlocculation of dimorphic yeast benjaminiella poitrasii is alter aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB a1393-13950 v1013 a

A strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibited faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Atomic force microscopy revealed higher surface roughness of Y (439.34 rms) than Y-5 (52 rms). Also, the former had a zeta potential of -65.97 +/- 3.45 as against -50.21 +/- 2.49 for the latter. Flocculation of both Y and Y-5 could be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation was promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing. (C) 2009 Elsevier Ltd. All rights reserved.

10aBenjaminiella poitrasii10adimorphism10aflocculation10aNAD-glutamate dehydrogenase1 aJoshi, C., V.1 aGhormade, Vandana1 aKunde, P.1 aKulkarni, P.1 aMamgain, H.1 aBhat, Suresh, K.1 aPaknikar, K., M.1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/flocculation-dimorphic-yeast-benjaminiella-poitrasii-altered-modulation-nad-glutamate-002552nas a2200289 4500008004100000022001400041245018000055210006900235260007400304300001000378490000800388520141500396653002101811653002801832653004001860653002101900653003201921653002401953653003801977100001802015700001902033700002002052700001702072700002102089700002602110856012602136 2013 eng d a0003-607200aBiochemical correlate of dimorphism in a zygomycete benjaminiella poitrasii: characterization of purified NAD-dependent glutamate dehydrogenase, a target for antifungal agents0 aBiochemical correlate of dimorphism in a zygomycete benjaminiell aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJUL a25-360 v1043 a

The fungal organisms, especially pathogens, change their vegetative (Y, unicellular yeast and H, hypha) morphology reversibly for survival and proliferation in the host environment. NAD-dependent glutamate dehydrogenase (NAD-GDH, EC 1.4.1.2) from a non-pathogenic dimorphic zygomycete Benjaminiella poitrasii was previously reported to be an important biochemical correlate of the transition process. The enzyme was purified to homogeneity and characterized. It is a 371 kDa native molecular weight protein made up of four identical subunits. Kinetic studies showed that unlike other NAD-GDHs, it may act as an anabolic enzyme and has more affinity towards 2-oxoglutarate than l-glutamate. Chemical modifications revealed the involvement of single histidine and lysine residues in the catalytic activity of the enzyme. The phosphorylation and dephosphorylation study showed that the NAD-GDH is present in active phosphorylated form in hyphal cells of B. poitrasii. Two of the 1,2,3 triazole linked beta-lactam-bile acid conjugates synthesized in the laboratory (B18, B20) were found to be potent inhibitors of purified NAD-GDH which also significantly affected Y-H transition in B. poitrasii. Furthermore, the compound B20 inhibited germ tube formation during Y-H transition in Candida albicans strains and Yarrowia lipolytica. The possible use of NAD-GDH as a target for antifungal agents is discussed.

10aAntifungal agent10aBenjaminiella poitrasii10aBiochemical correlate of dimorphism10aCandida albicans10aNAD-GDH activity regulation10aYarrowia lipolytica10aYeast-hypha reversible transition1 aJoshi, C., V.1 aPathan, E., K.1 aPunekar, N., S.1 aTupe, S., G.1 aKapadnis, B., P.1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/biochemical-correlate-dimorphism-zygomycete-benjaminiella-poitrasii-characterization-002431nas a2200277 4500008004100000022001400041245015100055210006900206260000800275300001100283490000700294520142900301653002801730653002101758653003301779653001501812653002301827653003701850653002701887100002101914700002201935700002301957700002101980700002602001856012602027 2019 eng d a1567-135600aMolecular studies of NAD- and NADP-glutamate dehydrogenases decipher the conundrum of yeast-hypha dimorphism in zygomycete Benjaminiella poitrasii0 aMolecular studies of NAD and NADPglutamate dehydrogenases deciph cDEC afoz0740 v193 a

Benjaminiella poitrasii, a zygomycete, shows glucose- and temperature-dependent yeast (Y)-hypha (H) dimorphic transition. Earlier, we reported the biochemical correlation of relative proportion of NAD- and NADP-glutamate dehydrogenases (GDHs) with Y-H transition. Further, we observed the presence of one NAD-GDH and two form-specific NADP-GDH isoenzymes in B. poitrasii. However, molecular studies are necessary to elucidate the explicit role of GDHs in regulating Y-H reversible transition. Here, we report the isolation and characterization of one NAD (BpNADGDH, 2.643 kb) and two separate genes, BpNADPGDH I (Y-form specific, 1.365 kb) and BpNADPGDH II (H-form specific, 1.368 kb) coding for NADP-GDH isoenzymes in B. poitrasii. The transcriptional profiling during Y-H transition showed higher BpNADPGDH I expression in Y cells while expression of BpNADPGDH II was higher in H cells. Moreover, the yeast-form monomorphic mutant (Y-5) did not show BpNADPGDH II expression under normal dimorphism triggering conditions. Transformation with H-form specific BpNADPGDH II induced the germ tube formation in Y-5, which confirmed the cause-effect relationship between BpNADPGDH genes and morphological outcome in B. poitrasii. Interestingly, expression of H-form specific BpNADPGDH II also induced germ tube formation in human pathogenic, non-dimorphic yeast Candida glabrata, which further corroborated our findings.

10aBenjaminiella poitrasii10aCandida glabrata10adifferential gene expression10adimorphism10amonomorphic mutant10aNAD/NADP-glutamate dehydrogenase10ayeast-hypha transition1 aPathan, Ejaj, K.1 aGhormade, Vandana1 aPanwar, Sneh, Lata1 aPrasad, Rajendra1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/molecular-studies-nad-and-nadp-glutamate-dehydrogenases-decipher-conundrum-yeast-hypha