Piotr Borsuk, Anna Przykorska, Karina Blachnio, Michal Koper, Jerzy M. Pawlowicz, Malgorzata Pekala, Piotr Weglenski
l-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans
Expression of the arginase structural gene (agaA) in Aspergillus nidulans is subject to complex transcriptional and post-transcriptional regulation. Arginase mRNA has a long 5?-UTR sequence. Analysis of this sequence in silico revealed its putative complex secondary structure, the presence of arginine-binding motifs (arginine aptamers) and a short intron with two potential 3? splicing sites. In this report we present evidence that L-arginine (i) binds directly to the arginase 5?-UTR; (ii) invokes drastic changes in the secondary structure of the 5?-UTR, unlike several other L-amino acids and D-arginine; and (iii) forces the selection of one of two 3? splice sites of an intron present in the 5?-UTR. We postulate that expression of the eukaryotic structural gene coding for arginase in A. nidulans is regulated at the level of mRNA stability, depending on riboswitch-mediated alternative splicing of the 5?-UTR intron.
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 388, 02/2007
Pages: 135 - 144
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