AI Article Synopsis
- The study identifies a gene from sp. NKBG15041c that improves stress tolerance by encoding a MoxR AAA+ ATPase, named SyMRP.
- SyMRP exhibits weak ATPase activity and protects certain proteins from heat-induced aggregation, functioning as a chaperone in an ATP-dependent manner.
- Although it forms a stable hexamer, its structure differs from the typical AAA+ ATPase ring, as evidenced by microscopy techniques and SAXS analysis.
Article Abstract
We isolated a stress-tolerance-related gene from a genome library of sp. NKBG15041c. The expression of the gene in confers resistance against various stresses. The gene encodes a MoxR AAA+ ATPase, which was designated SyMRP since it belongs to the MRP subfamily. The recombinant SyMRP showed weak ATPase activity and protected citrate synthase from thermal aggregation. Interestingly, the chaperone activity of SyMRP is ATP-dependent. SyMRP exists as a stable hexamer, and ATP-dependent conformation changes were not detected via analytical ultracentrifugation (AUC) or small-angle X-ray scattering (SAXS). Although the hexameric structure predicted by AlphaFold 3 was the canonical flat-ring structure, the structures observed by atomic force microscopy (AFM) and transmission electron microscopy (TEM) were not the canonical ring structure. In addition, the experimental SAXS profiles did not show a peak that should exist in the symmetric-ring structure. Therefore, SyMRP seems to form a hexameric structure different from the canonical hexameric structure of AAA+ ATPase.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11432383 | PMC |
| http://dx.doi.org/10.3390/ijms25189955 | DOI Listing |
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