TY - JOUR
T1 - Structure of the Rho transcription terminator
T2 - Mechanism of mRNA recognition and helicase loading
AU - Skordalakes, Emmanuel
AU - Berger, James M.
N1 - Funding Information:
The authors are grateful to James Holton at Beamline 8.3.1 of the Advanced Light source for assistance with data acquisition and to David King for mass spectroscopy analyses. We would also like to thank James Keck, Deborah Fass, David Akey, Jan Erzberger, and Scott Gradia for critical reading the manuscript, as well as members of the Berger Lab for helpful discussions and insights. This work was supported by generous assistance from the G. Harold and Leila Y. Mathers Charitable Foundation.
PY - 2003/7/11
Y1 - 2003/7/11
N2 - In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 Å resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites - a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding - point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 Å) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.
AB - In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 Å resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites - a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding - point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 Å) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.
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U2 - 10.1016/S0092-8674(03)00512-9
DO - 10.1016/S0092-8674(03)00512-9
M3 - Article
C2 - 12859904
AN - SCOPUS:0037559627
SN - 0092-8674
VL - 114
SP - 135
EP - 146
JO - Cell
JF - Cell
IS - 1
ER -