Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 400, Issue 1, Pages 16-23Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.05.004
Keywords
helicase; Rho factor; RNA capture mechanism; transcription termination; X-ray crystal structure
Categories
Funding
- Ministerio de Educacion y Ciencia de Espana [BFU2005-24123-E, BFU2008-02372/BMC, BIO2006-14139, BIO2009-10576]
- Generalitat de Catalunya [2009SGR-1309]
- EU [LSHG-2006-031220, LSHG-CT-2005-512028]
- Fundacio La Marato de TV3 [052810]
- European Synchrotron Radiation Facility
- ICREA Funding Source: Custom
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The Rho factor is a ring-shaped ATP-dependent helicase that mediates transcription termination in most prokaryotic cells by disengaging the transcription elongation complex formed by the RNA polymerase, DNA, and the nascent RNA transcript. The crystal structures of key intermediates along the kinetic pathway of RNA binding to Rho unveiled an unprecedented mode of helicase loading and provided a model for the ATP turnover coupled to coordinated strand movement. Here we report the structure of the early RNA-free state of Rho, which had eluded crystallization for many years but now completes the series. The structure allows the characterization of the apo-form Rho from Thermotoga maritima to 2.3 angstrom resolution, reveals an RNA-recruiting site that becomes hidden after occupancy of the adjacent specific primary RNA-binding site, and suggests an enriched model for mRNA capture that is consistent with previous data. (C) 2010 Elsevier Ltd. All rights reserved.
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