Molecular studies of NAD- and NADP-glutamate dehydrogenases decipher the conundrum of yeast-hypha dimorphism in zygomycete Benjaminiella poitrasii.


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
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.

Auteurs

Ejaj K Pathan (EK)

Biochemical Sciences Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, Maharashtra, India.

Vandana Ghormade (V)

Nanobioscience Group, Agharkar Research Institute, GG Agarkar Road, Pune 411004, Maharashtra, India.

Sneh Lata Panwar (SL)

School of Life Sciences, Jawaharlal Nehru University, New Mehrauli Road, New Delhi 110067, India.

Rajendra Prasad (R)

School of Life Sciences, Jawaharlal Nehru University, New Mehrauli Road, New Delhi 110067, India.
Amity University Haryana, Amity Education Valley, Manesar, Gurugram 122413, Haryana, India.

Mukund V Deshpande (MV)

Biochemical Sciences Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, Maharashtra, India.

Articles similaires

Biofilms Candida albicans Quorum Sensing Candida glabrata Menthol
Ascomycota Cenchrus Chromosomes, Fungal Genome, Fungal Plant Diseases
Animals Wound Healing Mice Wearable Electronic Devices Wound Infection

Classifications MeSH