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AtAAH encodes a protein with allantoate amidohydrolase activity from Arabidopsis thaliana

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Abstract

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.

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Acknowledgments

This work was supported by funds from grant no. 2003-00779, NRI, CSREES, USDA awarded to JCP. CDT was supported by a Natural Sciences and Engineering Research Council of Canada Post-Doctoral Fellowship and a University of Missouri Life Sciences Post-Doctoral Fellowship.

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Authors and Affiliations

  1. Department of Biochemistry and Interdisciplinary Plant Group, University of Missouri, 117 Schweitzer Hall, Columbia, MO, 65211, USA

    Christopher D. Todd & Joe C. Polacco

  2. Department of Biology, University of Saskatchewan, 112 Science Place, S7N 5E2, Saskatoon, Sask, Canada

    Christopher D. Todd

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  1. Christopher D. Todd
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  2. Joe C. Polacco
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Correspondence to Christopher D. Todd.

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Todd, C.D., Polacco, J.C. AtAAH encodes a protein with allantoate amidohydrolase activity from Arabidopsis thaliana. Planta 223, 1108–1113 (2006). https://doi.org/10.1007/s00425-006-0236-x

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  • DOI: https://doi.org/10.1007/s00425-006-0236-x

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