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JXB Advance Access originally published online on November 8, 2004
Journal of Experimental Botany 2005 56(409):91-99; doi:10.1093/jxb/eri014
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Journal of Experimental Botany, Vol. 56, No. 409, © Society for Experimental Biology 2005; all rights reserved

RESEARCH PAPER

Analysis of two alleles of the urease gene from potato: polymorphisms, expression, and extensive alternative splicing of the corresponding mRNA

Claus-Peter Witte *, Sarah Tiller, Edwige Isidore, Howard V. Davies and Mark A. Taylor{dagger}

Scottish Crop Research Institute, Unit of Plant Biochemistry, Invergowrie, Dundee DD2 5DA, UK

{dagger} To whom correspondence should be addressed. Fax: +44 (0)1382 562426. E-mail: mtaylo{at}scri.sari.ac.uk

Globally, urea is the most widely used nitrogen fertilizer and is made accessible to plants via the urease reaction. However, sequence information for the plant enzyme is scarce. A cDNA encoding urease from soybean (Glycine max) has been cloned and sequence information has been obtained for two alleles (11 and 19 kbp, respectively) of the potato (Solanum tuberosum, cv. Désirée) urease gene and the corresponding cDNAs. It was found that urease is encoded by a single copy gene in several solanaceous species, and maps to chromosome V in potato. By contrast, the presence of two urease genes was reported for soybean. Comparative analysis of 11 kbp overlapping allelic DNA allowed the quantification of single nucleotide polymorphisms and revealed the presence of a truncated Ty1-copia retrotransposon in one of the alleles. Both alleles contained a copy of a terminal-repeat retrotransposon in miniature (TRIM). 25–50% of urease pre-mRNAs from both alleles were alternatively spliced in a variety of different ways. The retrotransposons had no effect on splicing. While urease is expressed in all tissues tested, its mRNA and protein are of low abundance. The TATA-less urease promoter appears to drive low-level housekeeping transcription. An in silico analysis showed that eukaryotic urease protein sequences are very similar to sequences from prokaryotic enzymes, conserving all residues of known functional importance. It is therefore likely that all known ureases are structurally similar, employing the same catalytic mechanism.

Key words: Adenylate kinase, alternative splicing, SNP, TRIM, Ty1-copia, urease


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