| Autor: |
Borsuk, Piotr, Przykorska, Anna, Blachnio, Karina, Koper, Michal, Pawlowicz, Jerzy M., Pekala, Malgorzata, Weglenski, Piotr |
| Předmět: |
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| Zdroj: |
Biological Chemistry; Feb2007, Vol. 388 Issue 2, p135-144, 10p, 8 Black and White Photographs, 1 Diagram, 5 Graphs |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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