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l-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans by Piotr Borsuk; Anna Przykorska; Karina Blachnio; Michal Koper; Jerzy M. Pawlowicz; Malgorzata Pekala; Piotr Weglenski is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is l-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans about?

Expression of the arginase structural gene (agaA) in Aspergillus nidulans is subject to complex transcriptional and post-transcriptional regulation. Arginase mRNA has a long 59-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 39 splicing sites. In this report we present evidence that L-arginine (i) binds directly to the arginase 59-UTR; (ii) invokes drastic changes in the secondary structure of the 59-UTR, unlike several other L-amino acids and D-arginine; and (iii) forces the selection of one of two 39 splice sites of an intron present in the 59-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 59-UTR intron.

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Author

Piotr Borsuk; Anna Przykorska; Karina Blachnio; Michal Koper; Jerzy M. Pawlowicz; Malgorzata Pekala; Piotr Weglenski

Publisher

Walter de Gruyter GmbH

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)