02015nas a2200277   4500008004100000022001400041245011600055210006900171260009900240300001400339490000800353520100300361653002801364653001501392653001701407653003201424100001801456700002201474700001401496700001701510700001601527700002101543700002101564700002601585856012601611       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<p>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.</p>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.  uhttp://library.ncl.res.in/content/flocculation-dimorphic-yeast-benjaminiella-poitrasii-altered-modulation-nad-glutamate-002430nas a2200277   4500008004100000022001400041245015100055210006900206260000800275300001100283490000700294520142900301653002801730653002101758653003301779653001501812653002301827653003701850653002701887100002101914700002201935700002301957700002101980700002602001856012502027       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<p>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.</p>
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.  uhttp://library.ncl.res.in/content/molecular-studies-nad-and-nadp-glutamate-dehydrogenases-decipher-conundrum-yeast-hypha