Abstract
The mammalian 5′-AMP-activated protein kinase (AMPK) is a heterotrimeric protein consisting of α-, β- and γ-subunits. The α-subunit is the catalytic subunit. The non-catalytic subunits AMPK-β and AMPK-γ form, together with the catalytic AMPK-α, the active kinase complex in mammals and its homologue in yeast. The gene for AMPK-γ-1 has been designated recently as PRKAG1. We have isolated mouse Prkag1 cDNA from testis (1623 nt) coding for 330 aa and we have shown its ubiquitous expression as a 1.8-kb transcript. A comparison between mouse, rat and human PRKAG1 cDNA and protein sequences shows that the gene is highly conserved among these species with a homology of 96% at the protein level. Southern blot analysis indicates that there is more than one gene for PRKAG in the mouse genome. Prkag1 contains 12 exons with short introns. Analysis of 50 interspecific backcross mice mapped the mouse gene to the distal region of chromosome 15.
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