Abstract：
:AAA+ proteins (ATPases associated with various cellular activities) are oligomeric ATPases that use ATP hydrolysis to remodel their substrates. By similarity with GTPases, a dynamic organization of the nucleotide-binding pockets between ATPase protomers is proposed to regulate functionality. Using the transcription activator PspF as an AAA+ model, we investigated contributions of conserved residues for roles in ATP hydrolysis and intersubunit communication. We determined the R-finger residue and revealed that it resides in a conserved "R-hand" motif (R(x)D(xxx)R) needed for its "trans-acting" activity. Further, a divergent Walker A glutamic acid residue acts synergistically with a tyrosine residue to function in ADP-dependent subunit-subunit coordination, forming the "ADP-switch" motif. Another glutamic acid controls hexamer formation in the presence of nucleotides. Together, these results lead to a "residue-nucleotide" interaction map upon which to base AAA+ core regulation.
journal_name
Mol Celljournal_title
Molecular cellauthors
Joly N,Zhang N,Buck Mdoi
10.1016/j.molcel.2012.06.012subject
Has Abstractpub_date
2012-08-10 00:00:00pages
484-90issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(12)00507-2journal_volume
47pub_type
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