Disease relevance of ARG80

• The control region and part of the coding sequence of the ARGR genes were fused to the Escherichia coli lacZ gene [1].

High impact information on ARG80

• Furthermore, we show that like p62TCF, Elk-1 forms complexes with the yeast SRF-homologue MCM1 but not with yeast ARG80 [2].
• ARG80 and Agamous exhibit similar DNA binding specificities but do not interact with either STE12 or p62TCF [3].
• Through the analysis of promoter constructs with ARC deleted and an arg80 rad6 double mutant, we show that Rad6 repression is mediated through the ArgR/Mcm1 complex [4].
• Swapping functional specificity of a MADS box protein: residues required for Arg80 regulation of arginine metabolism [5].
• It remains functional if the TATA box is moved downstream of it but becomes inoperative in repression when displaced to a far-upstream position where it mediates an arginine and ARGR-dependent induction of gene expression [6].

Biological context of ARG80

• MCM1 has striking homology to ARG80, a regulatory gene of the arginine metabolic pathway located about 700 base-pairs upstream from MCM1 [7].
• By in vitro mutagenesis we created point mutations and deletions in the 5' non-coding region of the ARG5,6 gene which allowed us to define the primary target of ARGR control [8].

Associations of ARG80 with chemical compounds

• We show here that Mcm1p and Arg80p chaperoning by Arg82p does not involve the inositol polyphosphate kinase activity of Arg82p, but requires its polyaspartate domain [9].

Physical interactions of ARG80

• With the support of chromatin IP chip data, we also predict a possible variant of the Swi4 binding motif and recover a core motif for Arg80 [10].

Regulatory relationships of ARG80

• Arg82p also controls expression of arginine-responsive genes by interacting with Arg80p and Mcm1p, and expression of Mcm1-dependent genes by interacting with Mcm1p [9].

Other interactions of ARG80

• The UASI-protein complex was also observed even when extracts were derived from arg80/argRI or arg81/argRII deletion mutants [11].
• In vitro studies of the binding of the ARGR proteins to the ARG5,6 promoter [12].
• Sequences in and around BoxA are necessary for ARGR binding to these four promoters in vitro, whereas sequences in and around BoxB are clearly protected against DNase I digestion only for CAR1 [13].
• A similar analysis of expression of the gene CPA1, for which a translational regulation by arginine has been clearly demonstrated (M. Werner, A. Feller, F. Messenguy, and A. Piérard, Cell 49:805-813, 1987), indicates that this gene is also partly regulated at the transcriptional level by the ARGR repressor system [14].

Analytical, diagnostic and therapeutic context of ARG80

• By gel retardation assay and DNase I footprinting analysis, we have determined precisely the target of the ARGR proteins [13].

References