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MBC in Press, published online ahead of print September 20, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0384

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Submitted on May 4, 2006
Revised on August 30, 2006
Accepted on September 7, 2006

The Structure of Escherichia coli Signal Recognition Particle Revealed by Scanning Transmission Electron Microscopy

Iain L. Mainprize,* Daniel R. Beniac,{dagger} Elena Falkovskaia,{ddagger} Robert M. Cleverley,{sect} Lila M. Gierasch,{ddagger} F. Peter Ottensmeyer,|| and David W. Andrews*

*Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, L8N 3Z5, Canada; {dagger}National Microbiology Laboratory, Canadian Science Centre for Human and Animal Health, Winnipeg, R3E 3R2, Canada; {ddagger}Departments of Biochemistry and Molecular Biology and Chemistry, University of Massachusetts, Amherst, MA 01003; {sect}Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom; ||Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, M5G 2M9, Canada

Monitoring Editor: Peter Walter

Structural studies on various domains of the ribonucleoprotein signal recognition particle (SRP) have not converged on a single complete structure of bacterial SRP consistent with the biochemistry of the particle. We obtained a three-dimensional structure for E. coli SRP by cryo-scanning transmission electron microscopy and mapped the internal RNA by electron spectroscopic imaging. Crystallographic data were fit into the SRP reconstruction and although the resulting model differed from previous models, they could be rationalized by movement through an interdomain linker of Ffh, the protein component of SRP. Fluorescence resonance energy transfer experiments determined interdomain distances consistent with our model of SRP. Docking our model onto the bacterial ribosome suggests a mechanism for signal recognition involving interdomain movement of Ffh into and out of the nascent chain exit site and suggests how SRP could interact and/or compete with the ribosome-bound chaperone, trigger factor, for a nascent chain during translation.

Address correspondence to: David W. Andrews (andrewsd{at}mcmaster.ca)




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N. Bradshaw and P. Walter
The Signal Recognition Particle (SRP) RNA Links Conformational Changes in the SRP to Protein Targeting
Mol. Biol. Cell, July 1, 2007; 18(7): 2728 - 2734.
[Abstract] [Full Text] [PDF]


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