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

被引：14

作者：

Deveze-Alvarez, M ^{[1
]}

García-Soto, J ^{[1
]}

Martínez-Cadena, G ^{[1
]}

机构：

[1] Univ Guanajuato, Fac Quim, Inst Invest Biol Expt, Guanajuato 36000, Gto, Mexico

来源：

MICROBIOLOGY-SGM | 2001年 / 147卷

关键词：

regulation; spores; germination; zygomycete; GAPDH;

D O I：

10.1099/00221287-147-9-2579

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 [P-32]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 A blakesleeanus is proposed.

引用

页码：2579 / 2584

页数：6

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