Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 147 (2001), 2579-2584
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Deveze-Alvarez, M.
Right arrow Articles by Martínez-Cadena, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Deveze-Alvarez, M.
Right arrow Articles by Martínez-Cadena, G.
Agricola
Right arrow Articles by Deveze-Alvarez, M.
Right arrow Articles by Martínez-Cadena, G.
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




This article has been cited by other articles:


Home page
DiabetesHome page
M. Kanwar and R. A. Kowluru
Role of Glyceraldehyde 3-Phosphate Dehydrogenase in the Development and Progression of Diabetic Retinopathy
Diabetes, January 1, 2009; 58(1): 227 - 234.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2001 Society for General Microbiology.