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Microbiology (2001), 147, 2579-2584.
© 2001 Society for General Microbiology

Biochemistry

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

Martha Deveze-Alvarez1, Jesús García-Soto1 and Guadalupe Martínez-Cadena1

Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Apdo. postal 187, Guanajuato, Gto, 36000, Mexico1

Author for correspondence: Guadalupe Martínez-Cadena. Tel: +52 473 24302 8164. Fax: +52 473 24302 8153. 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 [32P]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






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Copyright © 2001 Society for General Microbiology.