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Vrentas CE Gaal T Berkmen MB Rutherford ST Haugen SP Vassylyev DG Ross W Gourse RL 《Journal of molecular biology》2008,377(2):551-564
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Daniel J. Koslover Furqan M. Fazal Rachel A. MooneyRobert Landick Steven M. Block 《Journal of molecular biology》2012,423(5):664-676
Rho termination factor is an essential hexameric helicase responsible for terminating 20-50% of all mRNA synthesis in Escherichia coli. We used single-molecule force spectroscopy to investigate Rho-RNA binding interactions at the Rho utilization site of the λtR1 terminator. Our results are consistent with Rho complexes adopting two states: one that binds 57 ± 2 nt of RNA across all six of the Rho primary binding sites, and another that binds 85 ± 2 nt at the six primary sites plus a single secondary site situated at the center of the hexamer. The single-molecule data serve to establish that Rho translocates 5′ → 3′ toward RNA polymerase (RNAP) by a tethered-tracking mechanism, looping out the intervening RNA between the Rho utilization site and RNAP. These findings lead to a general model for Rho binding and translocation and establish a novel experimental approach that should facilitate additional single-molecule studies of RNA-binding proteins. 相似文献
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