Martin R Pool
Affiliation: University of Manchester
- A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocaseMartin 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...
- 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...
- Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocationJane 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...
- Signal recognition particle mediates post-translational targeting in eukaryotesBenjamin 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...
- N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumGabriella 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...
- Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulumBenedict 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...
- Following the signal sequence from ribosomal tunnel exit to signal recognition particleMario 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...
- Signal recognition particle receptor exposes the ribosomal translocon binding siteMario Halic
Institute of Biochemistry, Charit, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany
Science 312:745-7. 2006....
- Structure of the signal recognition particle interacting with the elongation-arrested ribosomeMario Halic
Institute of Biochemistry, Charite, University Medical School, Humboldt University of Berlin, Monbijoustrasse 2, 10117 Berlin, Germany
Nature 427:808-14. 2004....
- Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognitionLionel Terzi
, , , Switzerland
Biochemistry 43:107-17. 2004..Hence, these studies reveal differential modes of SRP-ribosome interactions mediated by the Alu domain...
- Distinct modes of signal recognition particle interaction with the ribosomeMartin 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...