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Example sentences for: midasin
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Tagging of the midasin gene in yeast
The AAA domain of midasin is evolutionarily related to that of dynein, but it appears to lack a microtubule-binding site.
One possibility is that the MIDAS site serves to attach protein ligands through a mechanism involving participation of a glutamate or aspartate residue on the ligand in the coordination of a Mg 2+ion at the MIDAS site of midasin, in a manner similar to that by which the MIDAS site in integrin I-domains appears to mediate attachment of collagen through the glutamate in the GFOGER binding motif [ 36 ] . Interestingly, the related RGE ligand-binding motif [ 41 ] occurs in a conserved region of the midasin AAA-domain (yeast, residues 1835-1838), as well as in the AAA-domain of Mg chelatases [ 32 ] . The presence of this consensus binding motif in the AAA domain raises the possibility of the midasin molecule folding back onto itself, with the M-domain becoming attached to one face of the AAA domain and perhaps regulating access to its central chamber, in a manner analogous to that in which the 19S proteasome regulator, also an AAA protein, controls access to the central proteolytic chamber of the proteasome [ 42 ] .
Relationship of midasin to other AAA proteins
In all the available organisms, the four central protomers of the midasin polypeptide, AAA2, AAA3, AAA4 and AAA5, possess canonical Walker A and B motifs, as well as the critical Asn in sensor 1 and Arg in sensor 2 that are required for proper function in other AAA proteins [ 15 ] . The presence of these critical residues, taken together with their higher level of average sequence conservation (Table 1), suggests that the four central protomers all retain an active enzymatic function.
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