| Mss116 plays roles in the assembly of the mitochondrial translational machinery as well as in the translation process itself. | The DEAD-box helicase Mss116 plays distinct roles in mitochondrial ribogenesis and mRNA-specific translation.
De Silva D, Poliquin S, Zeng R, Zamudio-Ochoa A, Marrero N, Perez-Martinez X, Fontanesi F, Barrientos A., Free PMC Article | 11/11/2017 |
| Crystal structures of MSS116 reveal that core stability is modulated by family-specific interactions that favor certain RNA or DNA substrates. | Molecular insights into RNA and DNA helicase evolution from the determinants of specificity for a DEAD-box RNA helicase.
Mallam AL, Sidote DJ, Lambowitz AM., Free PMC Article | 09/12/2015 |
| 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. | Yeast DEAD box protein Mss116p is a transcription elongation factor that modulates the activity of mitochondrial RNA polymerase.
Markov DA, Wojtas ID, Tessitore K, Henderson S, McAllister WT., Free PMC Article | 08/9/2014 |
| The two strands of double strands RNA are recognized asymmetrically by the RNA-structure modulating Mss116p. | Exploring the molecular basis of dsRNA recognition by Mss116p using molecular dynamics simulations and free-energy calculations.
Xue Q, Zhang JL, Zheng QC, Cui YL, Chen L, Chu WT, Zhang HX. | 03/22/2014 |
| Mss116 stabilizes an early, obligate folding intermediate within intron domain 1. | The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate.
Fedorova O, Pyle AM., Free PMC Article | 01/26/2013 |
| results provide a comprehensive structural model for how DEAD-box proteins (like Mss116) recognize and unwind RNA duplexes | Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p.
Mallam AL, Del Campo M, Gilman B, Sidote DJ, Lambowitz AM., Free PMC Article | 12/8/2012 |
| a critical activity in the Mss116p-mediated folding of the aI5-gamma intron is ATP-dependent RNA-unwinding activity. | ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo.
Potratz JP, Del Campo M, Wolf RZ, Lambowitz AM, Russell R., Free PMC Article | 10/8/2011 |
| 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. | Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins.
Cao W, Coman MM, Ding S, Henn A, Middleton ER, Bradley MJ, Rhoades E, Hackney DD, Pyle AM, De La Cruz EM., Free PMC Article | 08/6/2011 |
| 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. | Dual roles for the Mss116 cofactor during splicing of the ai5γ group II intron.
Zingler N, Solem A, Pyle AM., Free PMC Article | 01/1/2011 |
| 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. | Structure-guided mutational analysis of a yeast DEAD-box protein involved in mitochondrial RNA splicing.
Bifano AL, Turk EM, Caprara MG., Free PMC Article | 05/3/2010 |
| Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. | Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA.
Del Campo M, Lambowitz AM., Free PMC Article | 01/21/2010 |
| 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. | Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones.
Del Campo M, Mohr S, Jiang Y, Jia H, Jankowsky E, Lambowitz AM., Free PMC Article | 01/21/2010 |
| DEAD-box proteins CYT-19, Mss116p, and Ded1p can achieve complete strand separation using a single ATP | DEAD-box proteins can completely separate an RNA duplex using a single ATP.
Chen Y, Potratz JP, Tijerina P, Del Campo M, Lambowitz AM, Russell R., Free PMC Article | 01/21/2010 |
| 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. | ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding.
Liu F, Putnam A, Jankowsky E., Free PMC Article | 01/21/2010 |
| 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. | A DExH/D-box protein coordinates the two steps of splicing in a group I intron.
Bifano AL, Caprara MG., Free PMC Article | 01/21/2010 |
| 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 | Do DEAD-box proteins promote group II intron splicing without unwinding RNA?
Del Campo M, Tijerina P, Bhaskaran H, Mohr S, Yang Q, Jankowsky E, Russell R, Lambowitz AM., Free PMC Article | 01/21/2010 |
| Function of the C-terminal domain of the DEAD-box protein MSS116 is analyzed in vivo and in vitro. | Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro.
Mohr G, Del Campo M, Mohr S, Yang Q, Jia H, Jankowsky E, Lambowitz AM., Free PMC Article | 01/21/2010 |
| Duplex unwinding by Ded1/Mss116 is based on local destabilization of RNA helical regions. | DEAD-box proteins unwind duplexes by local strand separation.
Yang Q, Del Campo M, Lambowitz AM, Jankowsky E. | 01/21/2010 |
| Mss116p, like CYT-19, can act broadly as an RNA chaperone to stimulate the splicing of diverse group I and group II introns. | Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity.
Halls C, Mohr S, Del Campo M, Yang Q, Jankowsky E, Lambowitz AM., Free PMC Article | 01/21/2010 |
| 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. | A DEAD protein that activates intron self-splicing without unwinding RNA.
Solem A, Zingler N, Pyle AM. | 01/21/2010 |