Glyceraldehyde-3-phosphate dehydrogenase is negatively regulated by ADP-ribosylation in the fungus Phycomyces blakesleeanus

• Published in: Microbiology (Society for General Microbiology) 2001-09, Vol.147 (9), p.2579-2584
• Main Authors: Deveze-Alvarez, Martha, Garcia-Soto, Jesus, Martinez-Cadena, Guadalupe
• Format: Article
• Language: English
• Subjects: Adenosine Diphosphate Ribose - metabolism; ADP-ribosylation; Arginine - chemistry; glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism; Models, Biological; Molecular Weight; NAD - metabolism; Phycomyces - enzymology; Phycomyces - physiology; Phycomyces blakesleeanus; Protein Processing, Post-Translational; Spores, Fungal - enzymology
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/00221287-147-9-2579

Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Apdo. postal 187, Guanajuato, Gto, 36000, Mexico 1 Author for correspondence: Guadalupe Martínez-Cadena. Tel: [phone]. Fax: [phone]. e-mail: margua{at}quijote.ugto.mx Dormant spores of Phycomyces blakesleeanus contain a 37 kDa protein that is endogenously mono-ADP-ribosylated. This protein was purified and identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by N-terminal sequencing and homology analysis. GAPDH enzymic activity changed dramatically upon spore germination, being maximal at stages where ADP-ribosylation was nearly undetectable. The presence of glyceraldehyde 3-phosphate in this reaction affected the [ 32 P]ADP-ribosylation of the GAPDH. ADP-ribosylation of the GAPDH occurred by transfer of the ADP-ribose moiety from NAD to an arginine residue. A model for the regulation of GAPDH activity and its role in spore germination in P. blakesleeanus is proposed. Keywords: regulation, spores, germination, zygomycete, GAPDH Abbreviations: GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GA3P, glyceraldehyde 3-phosphate