MSS116 Antibody

1. Mss116 plays roles in the assembly of the mitochondrial translational machinery as well as in the translation process itself. PMID: 28520979
2. Crystal structures of MSS116 reveal that core stability is modulated by family-specific interactions that favor certain RNA or DNA substrates. PMID: 25497230
3. overexpression of RPO41 or MSS116 increases cell survival from colonies that were exposed to low temperature, suggesting a role for Mss116p in enhancing the efficiency of mitochondrial transcription under stress conditions. PMID: 24732805
4. The two strands of double strands RNA are recognized asymmetrically by the RNA-structure modulating Mss116p. PMID: 23895307
5. Mss116 stabilizes an early, obligate folding intermediate within intron domain 1. PMID: 22705286
6. results provide a comprehensive structural model for how DEAD-box proteins (like Mss116) recognize and unwind RNA duplexes PMID: 22940866
7. a critical activity in the Mss116p-mediated folding of the aI5-gamma intron is ATP-dependent RNA-unwinding activity. PMID: 21679717
8. We measured the rate and equilibrium constants underlying Mss116 ATP utilization and nucleotide-linked RNA binding. RNA accelerates the Mss116 steady-state ATPase approximately 7- fold by promoting rate-limiting ATP hydrolysis. PMID: 21501623
9. The Mss116 protein stimulates group II intron self-splicing in vitro through two distinct mechanisms that can be differentiated by varying the length of precursor exons and examining the function of protein mutants. PMID: 20554854
10. Together, these observations suggest that the efficiency by which Mss116p catalyzes the hydrolysis of ATP is critical for all of its splicing functions in vivo. PMID: 20307546
11. Mss116p, like CYT-19, can act broadly as an RNA chaperone to stimulate the splicing of diverse group I and group II introns. PMID: 17081564
12. This finding indicates that Mss116 is unlikely to promote intron splicing through the unwinding of kinetic traps. We propose that Mss116 promotes the ordered assembly of large RNA molecules through stabilization of on-pathway intermediates. PMID: 17188036
13. findings favor the hypothesis that DEAD-box proteins function in group II intron splicing as in other processes by using their unwinding activity to act as RNA chaperones PMID: 17936712
14. Duplex unwinding by Ded1/Mss116 is based on local destabilization of RNA helical regions. PMID: 17964264
15. Function of the C-terminal domain of the DEAD-box protein MSS116 is analyzed in vivo and in vitro. PMID: 18096186
16. Data suggest that Mrs1p stabilizes RNA structure and promotes the first step in splicing, while Mss116p acts after the first step and, utilizing ATP hydrolysis, specifically enhances the efficiency of exon ligation. PMID: 18789947
17. DEAD-box proteins CYT-19, Mss116p, and Ded1p can achieve complete strand separation using a single ATP PMID: 19088196
18. the energy from ATP hydrolysis is dispensable for strand separation. ATP binding, however, appears necessary. ATP hydrolysis is found to be required for fast enzyme release from the RNA and multiple substrate turnovers and thus for enzyme recycling. PMID: 19088201
19. Results suggest that DEAD-box proteins such as Mss116 and Cyt-19 function as RNA chaperones by virtue of their RNA-unwinding mechanism, which enables refolding of localized RNA regions or structures without globally disrupting RNA structure. PMID: 19393667
20. Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. PMID: 19748356

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KEGG: sce:YDR194C

STRING: 4932.YDR194C