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Example sentences for: protomers
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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.
There is no indication that any of these joining polypeptides contains a ATP-sensitive microtubule-binding site resembling that located between the AAA4 and AAA5 protomers of dynein [ 46 ] . The position of the N-terminal domain of midasin relative to the AAA domain is similar to that of the stem domain of dynein, and in several organisms the midasin N-terminal domain contains a cluster of basic residues that has the potential to bind microtubules in an ATP-insensitive manner.
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).
The essentially complete retention of the M-domain and the hexameric assembly of protomers in the AAA domain emphasizes the critical importance of these domains to the proper functioning of midasin.
It is notable that the functionally important Asn in sensor 1 and Arg in sensor 2 [ 15 ] are present and invariant among organisms in all protomers of midasin, except AAA1 and AAA6.
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