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Title: Structures of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus furiosus: Implications for the Targeting Step at the Membrane

Journal Article · · PLoS ONE
 [1];  [2];  [3];  [4];  [3];  [3]
  1. Univ. of California, San Francisco, CA (United States). Dept. of Biochemistry and Biophysics; DOE/OSTI
  2. SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
  3. Univ. of California, San Francisco, CA (United States). Dept. of Biochemistry and Biophysics
  4. Univ. of California, San Francisco, CA (United States). Dept. of Biochemistry and Biophysics; Rockefeller Univ., New York, NY (United States). Lab. of Cell Biology and Howard Hughes Medical Inst.

In all organisms, a ribonucleoprotein called the signal recognition particle (SRP) and its receptor (SR) target nascent proteins from the ribosome to the translocon for secretion or membrane insertion. We present the first X-ray structures of an archeal FtsY, the receptor from the hyper-thermophile Pyrococcus furiosus (Pfu), in its free and GDPNmagnesium-bound forms. The highly charged N-terminal domain of Pfu-FtsY is distinguished by a long N-terminal helix. The basic charges on the surface of this helix are likely to regulate interactions at the membrane. A peripheral GDP bound near a regulatory motif could indicate a site of interaction between the receptor and ribosomal or SRP RNAs. Small angle X-ray scattering and analytical ultracentrifugation indicate that the crystal structure of Pfu-FtsY correlates well with the average conformation in solution. Based on previous structures of two sub-complexes, we propose a model of the core of archeal and eukaryotic SRPNSR targeting complexes.

Research Organization:
SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Organization:
National Center for Research Resources (NCRR); National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
AC02-76SF00515
OSTI ID:
1627361
Journal Information:
PLoS ONE, Journal Name: PLoS ONE Journal Issue: 11 Vol. 3; ISSN 1932-6203
Publisher:
Public Library of ScienceCopyright Statement
Country of Publication:
United States
Language:
English

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  • Scwartz, Thomas U.; Schmidt, Daniel; Brohawn, Stephen G.
  • Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 18, 6823-6828 https://doi.org/10.3410/f.1032061.372725
journal May 2006

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Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle journal July 2011
Proposed Role for KaiC-Like ATPases as Major Signal Transduction Hubs in Archaea journal December 2017
Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor journal November 2009
GTPases and the origin of the ribosome journal January 2010
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes journal September 2010
Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle journal July 2011
Archaeal cell surface biogenesis journal June 2018