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Example sentences for: aaa
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The early evolutionary divergence of the different major branches of the AAA family makes it difficult to evaluate the phylogenetic relationships among them [ 45 ] . However, by restricting the analysis to residues in the more highly conserved regions of the AAA structure that interact directly with ATP, we have been able to improve the signal to noise ratio sufficiently to probe the phylogenetic relationship of midasin and dynein to representative members in other branches of the AAA family.
The initial step of the insertion can proceed in the presence of either Mg.ATP or a non-hydrolyzable ATP-analog and involves oligomerization of the BchD and BchI subunits to form an oligomeric ring of AAA protomers that resembles the ring structure of NSF and other AAA proteins [ 14 32 ] . The second step of the insertion involves an obligatory hydrolysis of ATP that is tightly coupled with the transfer of the chelated Mg 2+to the protoporphyrin ring by BchH [ 49 ] . Although the details differ from midasin, particularly with respect to the subunit composition of the AAA ring, this chelation reaction provides a structural model suggesting that the function of the midasin M-domain may be to regulate the ATPase activity of the AAA protomers in the pseudo-hexameric ring and thus couple ATP hydrolysis to the binding of a protein ligand at the MIDAS site.
gcP1 .66: GAT C TC GAT CCC GCG AAA TTA ATA CNN NNC ACT ATA GGG GAA TTG TGA GCG GAT AAC AAT TCC CCT (BglII site in bold; N indicates a random sequence region)
However, such primordial di-protomeric AAA polypeptides would have to have been simpler than those present in NSF, ClpA and p97 and other AAA proteins of the current era, for the latter assemble into two-tiered hexameric assemblies, with the axis joining the two protomers in each polypeptide oriented perpendicular to the plane of the hexameric ring [ 14 ] . We cannot, at present, exclude an alternative model for midasin structure in which the hexameric AAA ring assembly is a dimeric two-layered structure formed by two midasin polypeptides arranged laterally with all six odd-numbered protomers in one layer and all six even-numbered protomers in the other.
Such analysis of the AAA protomers that are best conserved among organisms (AAA2, AAA3, AAA4 and AAA5 in midasin, and AAA1 in dynein) shows that the AAA protomers of midasin and dynein are substantially more closely related to each other than they are to those in the other branches of the AAA family examined (Figs 7, 8).
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