ArticleMolecular cell2012
ATPase site architecture is required for self-assembly and remodeling activity of a hexameric AAA+ transcriptional activator.
Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- REC domain stabilizes the active heptamer of σiScience · 2023Article
- Revolving ATPase motors as asymmetrical hexamers in translocating lengthy dsDNA via conformational changes and electrostatic interactions in phi29, T7, herpesvirus, mimivirus,Exploration (Beijing, China) · 2023Review
- The heptameric structure of the flagellar regulatory protein FlrC is indispensable for ATPase activity and disassembled by cyclic-di-GMP.The Journal of biological chemistry · 2020Article
- Engineered CRISPRa enables programmable eukaryote-like gene activation in bacteria.Nature communications · 2019Article
- Hexameric assembly of the AAA+ protein McrB is necessary for GTPase activity.Nucleic acids research · 2019Article
- Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017Review
- Construction of Asymmetrical Hexameric Biomimetic Motors with Continuous Single-Directional Motion by Sequential Coordination.Small (Weinheim an der Bergstrasse, Germany) · 2017Article
- The Mutation of Glu at Amino Acid 3838 of AtMDN1 Provokes Pleiotropic Developmental Phenotypes in Arabidopsis.Scientific reports · 2016Article
- The bacterial enhancer-dependent RNA polymerase.The Biochemical journal · 2016Review
- An Arginine Finger Regulates the Sequential Action of Asymmetrical Hexameric ATPase in the Double-Stranded DNA Translocation Motor.Molecular and cellular biology · 2016Article
- TRANSCRIPTION. Structures of the RNA polymerase-σ54 reveal new and conserved regulatory strategies.Science (New York, N.Y.) · 2015Article
- Unique ATPase site architecture triggers cis-mediated synchronized ATP binding in heptameric AAA+-ATPase domain of flagellar regulatory protein FlrC.The Journal of biological chemistry · 2015Article
- Molecular basis of nucleotide-dependent substrate engagement and remodeling by an AAA+ activator.Nucleic acids research · 2014Article
- Interplay among Pseudomonas syringae HrpR, HrpS and HrpV proteins for regulation of the type III secretion system.FEMS microbiology letters · 2014Article
- Lytic water dynamics reveal evolutionarily conserved mechanisms of ATP hydrolysis by TIP49 AAA+ ATPases.Structure (London, England : 1993) · 2014Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
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Authors and funding
3 authors.
Funding
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.
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