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Updated: Sep 4, 2025

Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
Analysis of the Evolution of the MoxR ATPases
Vaibhav Bhandari1, David A J Van Ommen1, Keith S Wong1
1Department of Biochemistry, University of Toronto, Toronto, Ontario M5G 1M1, Canada.
Abstract:
MoxR proteins comprise a family of ATPases Associated with diverse cellular Activities (AAA+). These proteins are widespread and found across the diversity of prokaryotic species. Despite their ubiquity, members of the group remain poorly characterized. Only a few examples of MoxR proteins have been associated with cellular roles, where they have been shown to perform chaperone-like functions. A characteristic feature of MoxR proteins is their association with proteins containing the von Willebrand factor type A (VWA) domain. In an effort to understand the spread and diversity of the MoxR family, an evolutionary approach was undertaken. Phylogenetic techniques were used to define nine major subfamilies within the MoxR family. A combination of phylogenetic and genomic approaches was utilized to explore the extent of the partnership between the MoxR and VWA domain containing proteins (VWA proteins). These analyses led to the clarification of genetic linkages between MoxR and VWA proteins. A significant partnership is described here, as seven of nine MoxR subfamilies were found to be linked to VWA proteins. Available genomic data were also used to assess the intraprotein diversification of MoxR and VWA protein sequences. Data clearly indicated that, in MoxR proteins, the ATPase domain is maintained with high conservation while the remaining protein sequence evolves at a faster rate; a similar pattern was observed for the VWA domain in VWA proteins. Overall, our data present insights into the modular evolution of MoxR ATPases.
Insights
MoxR proteins, a family of ATPases Associated with diverse cellular Activities (AAA+), are widespread in prokaryotes but poorly understood. This study reveals evolutionary links between MoxR and VWA domain proteins, uncovering their modular evolution.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Molecular Biology
Background:
- MoxR proteins are ATPases Associated with diverse cellular Activities (AAA+) found widely in prokaryotes.
- Their cellular roles and diversity remain largely uncharacterized, with only a few known chaperone-like functions.
- MoxR proteins characteristically associate with proteins containing the von Willebrand factor A (VWA) domain.
Purpose of the Study:
- To investigate the evolutionary spread and diversity of the MoxR protein family.
- To explore the extent of the association between MoxR proteins and VWA domain proteins.
- To understand the patterns of sequence diversification within MoxR and VWA proteins.
Main Methods:
- Phylogenetic analysis to define MoxR subfamilies.
- Genomic analysis to identify genetic linkages between MoxR and VWA proteins.
- Comparative sequence analysis to assess intraprotein diversification.
Main Results:
- Nine major MoxR subfamilies were identified through phylogenetic analysis.
- Seven of the nine MoxR subfamilies show genetic linkage with VWA proteins.
- MoxR ATPases exhibit conserved ATPase domains and rapidly evolving accessory regions, a pattern mirrored in VWA proteins.
Conclusions:
- The study clarifies the evolutionary relationships and widespread partnership between MoxR and VWA proteins.
- Insights into the modular evolution of MoxR ATPases are provided.
- The findings contribute to a better understanding of MoxR protein function and diversity in prokaryotes.
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