Molecular studies of NAD- and NADP-glutamate dehydrogenases decipher the conundrum of yeast-hypha dimorphism in zygomycete Benjaminiella poitrasii.
Benjaminiella poitrasii
Candida glabrata
NAD/NADP-glutamate dehydrogenase
differential gene expression
dimorphism
monomorphic mutant
yeast–hypha transition
Journal
FEMS yeast research
ISSN: 1567-1364
Titre abrégé: FEMS Yeast Res
Pays: England
ID NLM: 101085384
Informations de publication
Date de publication:
01 12 2019
01 12 2019
Historique:
received:
21
03
2019
accepted:
22
10
2019
pubmed:
24
10
2019
medline:
17
6
2020
entrez:
24
10
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 31644791
pii: 5603745
doi: 10.1093/femsyr/foz074
pii:
doi:
Substances chimiques
Glutamates
0
NAD
0U46U6E8UK
NADP
53-59-8
Glutamate Dehydrogenase
EC 1.4.1.2
glutamate dehydrogenase (NAD(P)+)
EC 1.4.1.3
Glutamate Dehydrogenase (NADP+)
EC 1.4.1.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© FEMS 2019.