AtAAH encodes a protein with allantoate amidohydrolase activity from Arabidopsis thaliana

被引:45
作者
Todd, CD
Polacco, JC
机构
[1] Univ Saskatchewan, Dept Biol, Saskatoon, SK S7N 5E2, Canada
[2] Univ Missouri, Dept Biochem, Columbia, MO 65211 USA
[3] Univ Missouri, Interdisciplinary Plant Grp, Columbia, MO 65211 USA
关键词
allantoate amidohydrolase; AtAAH; HyuC; nitrogen metabolism; ureide; Arabidopsis thaliana;
D O I
10.1007/s00425-006-0236-x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
We report the identification and cloning of an allantoate amidohydrolase (allantoate deiminase, EC 3.5.3.9) cDNA from Arabidopsis thaliana (L.) Heynh. This sequence, which we term Arabidopsis thaliana Allantoate Amidohydrolase (AtAAH), was shown to be functional by complementation of Saccharomyces cerevisiae dal2 mutants, blocked in allantoate degradation. Following transfer to a medium containing allantoin as the sole nitrogen source, Ataah T-DNA insertion mutants were severely impaired and eventually died. Ataah mutants demonstrated higher allantoate levels than wild-type plants in the presence and absence of exogenous ureides, supporting a block in allantoate catabolism. AtAAH transcript was detected in all tissues examined by RT-PCR, consistent with a function in purine turnover in Arabidopsis. To our knowledge this is the first allantoate amidohydrolase gene identified in any plant species.
引用
收藏
页码:1108 / 1113
页数:6
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