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The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy.


ABSTRACT: 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 Escherichia coli SRP by cryoscanning 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 that were 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.

SUBMITTER: Mainprize IL 

PROVIDER: S-EPMC1679673 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

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The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy.

Mainprize Iain L IL   Beniac Daniel R DR   Falkovskaia Elena E   Cleverley Robert M RM   Gierasch Lila M LM   Ottensmeyer F Peter FP   Andrews David W DW  

Molecular biology of the cell 20060920 12


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 Escherichia coli SRP by cryoscanning 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  ...[more]

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