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ATPase Site Architecture Is Required for Self-Assembly and Remodeling Activity of a Hexameric AAA+ Transcriptional Activator
| Content Provider | PubMed Central |
|---|---|
| Author | Joly, Nicolas Zhang, Nan Buck, Martin |
| Copyright Year | 2012 |
| 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 (RxDxxxR) 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. |
| Related Links | http://dx.doi.org/10.1016/j.molcel.2012.06.012 |
| Starting Page | 484 |
| File Format | |
| ISSN | 10974164 |
| e-ISSN | 10974164 |
| Journal | Molecular Cell |
| Issue Number | 3-8 |
| Volume Number | 47 |
| Language | English |
| Publisher | Cell Press |
| Access Restriction | Open |
| Rights Holder | Cell Press |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology |
