Martin R Pool

Summary

Affiliation: University of Manchester
Country: UK

Publications

  1. pmc A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase
    Martin R Pool
    Faculty of Life Sciences, University of Manchester, Manchester M139PT, England, UK
    J Cell Biol 185:889-902. 2009
  2. ncbi request reprint Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review)
    Martin R Pool
    Faculty of Life Sciences, University of Manchester, Manchester, UK
    Mol Membr Biol 22:3-15. 2005
  3. pmc Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation
    Jane A Dalley
    Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, United Kingdom
    Mol Biol Cell 19:2876-84. 2008
  4. pmc Signal recognition particle mediates post-translational targeting in eukaryotes
    Benjamin M Abell
    School of Biological Sciences, University of Manchester, Manchester, UK
    EMBO J 23:2755-64. 2004
  5. pmc N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    Gabriella M A Forte
    Faculty of Life Sciences, University of Manchester, Manchester, United Kingdom
    PLoS Biol 9:e1001073. 2011
  6. pmc Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum
    Benedict C S Cross
    Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, M13 9PT, UK
    J Cell Sci 122:4393-400. 2009
  7. ncbi request reprint Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    Mario Halic
    Gene Center, Department of Chemistry and Biochemistry, University of Munich, Feodor Lynen Strasse 25, 81377 Munich, Germany
    Nature 444:507-11. 2006
  8. ncbi request reprint Signal recognition particle receptor exposes the ribosomal translocon binding site
    Mario Halic
    Institute of Biochemistry, Charite, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany
    Science 312:745-7. 2006
  9. ncbi request reprint Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    Mario Halic
    Institute of Biochemistry, Charite, University Medical School, Humboldt University of Berlin, Monbijoustrasse 2, 10117 Berlin, Germany
    Nature 427:808-14. 2004
  10. ncbi request reprint Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition
    Lionel Terzi
    Universite de Geneve, Departement de Biologie Cellulaire, CH 1211 Geneva 4, Switzerland
    Biochemistry 43:107-17. 2004

Collaborators

  • Eileithyia Swanton
  • Klemens Wild
  • Mario Halic
  • Irmgard Sinning
  • Roland Beckmann
  • Gabriella M A Forte
  • Benedict C S Cross
  • Jane A Dalley
  • Stephen High
  • Thorsten Mielke
  • Oliver Schlenker
  • Thomas Becker
  • Benjamin M Abell
  • Lionel Terzi
  • Colin J Stirling
  • Cornelia M Wilson
  • Anna C Callan
  • Catherine Rabu
  • Peristera Roboti
  • Craig McKibbin
  • Roger Whitehead
  • Michela Piacenti
  • Sabine L Flitsch
  • Alexander Selkirk
  • Marco Gartmann
  • Michael Blau
  • Katharina Strub
  • Robert A Grassucci
  • Joachim Frank
  • Christian M T Spahn
  • Bernhard Dobberstein

Detail Information

Publications11

  1. pmc A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase
    Martin R Pool
    Faculty of Life Sciences, University of Manchester, Manchester M139PT, England, UK
    J Cell Biol 185:889-902. 2009
    ..This suggests a signaling function for Rpl17 such that it can recognize a TM segment inside the ribosome and triggers rearrangements of the translocon, priming it for subsequent TM segment integration...
  2. ncbi request reprint Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review)
    Martin R Pool
    Faculty of Life Sciences, University of Manchester, Manchester, UK
    Mol Membr Biol 22:3-15. 2005
    ..Furthermore, the similarities and differences in the structure, function and cellular role of SRP in bacteria, chloroplasts, fungi and mammals will be stressed...
  3. pmc Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation
    Jane A Dalley
    Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, United Kingdom
    Mol Biol Cell 19:2876-84. 2008
    ..Overexpression of SRP can restore ribosome binding of SRP, but only partially rescues growth and translocation defects. Our results indicate that Rpl25p plays a critical role in the recruitment of SRP to the ribosome...
  4. pmc Signal recognition particle mediates post-translational targeting in eukaryotes
    Benjamin M Abell
    School of Biological Sciences, University of Manchester, Manchester, UK
    EMBO J 23:2755-64. 2004
    ..We find that dependency upon this SRP-dependent route is precursor specific, and propose a unifying model to describe the biogenesis of TA proteins in vivo...
  5. pmc N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    Gabriella M A Forte
    Faculty of Life Sciences, University of Manchester, Manchester, United Kingdom
    PLoS Biol 9:e1001073. 2011
    ..Hence N-terminal acetylation represents an early determining step in the cellular sorting of nascent polypeptides that appears to be conserved across a wide range of species...
  6. pmc Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum
    Benedict C S Cross
    Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester, M13 9PT, UK
    J Cell Sci 122:4393-400. 2009
    ..These results identify a novel effect of ES(I), and suggest that the drug can modulate canonical protein transport from the cytosol into the mammalian ER both in vitro and in vivo...
  7. ncbi request reprint Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    Mario Halic
    Gene Center, Department of Chemistry and Biochemistry, University of Munich, Feodor Lynen Strasse 25, 81377 Munich, Germany
    Nature 444:507-11. 2006
    ..These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting...
  8. ncbi request reprint Signal recognition particle receptor exposes the ribosomal translocon binding site
    Mario Halic
    Institute of Biochemistry, Charite, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany
    Science 312:745-7. 2006
    ....
  9. ncbi request reprint Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    Mario Halic
    Institute of Biochemistry, Charite, University Medical School, Humboldt University of Berlin, Monbijoustrasse 2, 10117 Berlin, Germany
    Nature 427:808-14. 2004
    ....
  10. ncbi request reprint Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition
    Lionel Terzi
    Universite de Geneve, Departement de Biologie Cellulaire, CH 1211 Geneva 4, Switzerland
    Biochemistry 43:107-17. 2004
    ..Hence, these studies reveal differential modes of SRP-ribosome interactions mediated by the Alu domain...
  11. ncbi request reprint Distinct modes of signal recognition particle interaction with the ribosome
    Martin R Pool
    Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, D 69120 Heidelberg, Germany
    Science 297:1345-8. 2002
    ..When SRP54 contacts SR, SRP54 is rearranged such that it is no longer close to L23a. This repositioning may allow the translocon to dock with the ribosome, leading to insertion of the signal peptide into the translocation channel...