SRP Keeps Polypeptides Translocation-Competent by Slowing Translation to Match Limiting ER-Targeting Sites

[1]  T. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes , 2007, Nature.

[2]  S. Rospert,et al.  Association of Protein Biogenesis Factors at the Yeast Ribosomal Tunnel Exit Is Affected by the Translational Status and Nascent Polypeptide Sequence* , 2007, Journal of Biological Chemistry.

[3]  K. Strub,et al.  Inefficient targeting to the endoplasmic reticulum by the signal recognition particle elicits selective defects in post-ER membrane trafficking. , 2007, Experimental cell research.

[4]  T. Rapoport,et al.  Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane. , 2006, Molecular biology of the cell.

[5]  J. Pelletier,et al.  Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A , 2006, Nature chemical biology.

[6]  P. Penczek,et al.  ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane , 2005, Nature Structural &Molecular Biology.

[7]  W. Nastainczyk,et al.  ERj1p has a basic role in protein biogenesis at the endoplasmic reticulum , 2005, Nature Structural &Molecular Biology.

[8]  S. Michaeli,et al.  The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: purification and functional analysis of its binding proteins by RNAi , 2005, Journal of Cell Science.

[9]  M. Pool Signal recognition particles in chloroplasts, bacteria, yeast and mammals (Review) , 2005, Molecular membrane biology.

[10]  R. Stroud,et al.  Mechanism of Association and Reciprocal Activation of Two GTPases , 2004, PLoS biology.

[11]  M. Jung,et al.  Protein transport into canine pancreatic microsomes: a quantitative approach. , 2004, European journal of biochemistry.

[12]  Arthur E Johnson,et al.  Cotranslational Membrane Protein Biogenesis at the Endoplasmic Reticulum* , 2004, Journal of Biological Chemistry.

[13]  Joachim Frank,et al.  Structure of the signal recognition particle interacting with the elongation-arrested ribosome , 2004, Nature.

[14]  M. Pool,et al.  Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition. , 2004, Biochemistry.

[15]  J. Flanagan,et al.  Signal Recognition Particle Binds to Ribosome-bound Signal Sequences with Fluorescence-detected Subnanomolar Affinity That Does Not Diminish as the Nascent Chain Lengthens* , 2003, The Journal of Biological Chemistry.

[16]  S. Michaeli,et al.  The Trypanosomatid Signal Recognition Particle Consists of Two RNA Molecules, a 7SL RNA Homologue and a Novel tRNA-like Molecule* , 2003, The Journal of Biological Chemistry.

[17]  V. Goder,et al.  In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site‐specific phosphorylation , 2000, The EMBO journal.

[18]  Oliver Weichenrieder,et al.  Structure and assembly of the Alu domain of the mammalian signal recognition particle , 2000, Nature.

[19]  Nicola Mason,et al.  Elongation arrest is a physiologically important function of signal recognition particle , 2000, The EMBO journal.

[20]  K. Strub,et al.  A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle. , 1997, Nucleic acids research.

[21]  P. Walter,et al.  Signal sequences specify the targeting route to the endoplasmic reticulum membrane , 1996, The Journal of cell biology.

[22]  T. Powers,et al.  The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome , 1996, Current Biology.

[23]  H. Lütcke,et al.  A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins. , 1995, The EMBO journal.

[24]  P. Walter,et al.  SRP samples nascent chains for the presenceof signal sequences by interacting with ribosomes at a discrete step during translation elongation , 1995, Cell.

[25]  H. Leffers,et al.  The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. , 1995, Molecular biology of the cell.

[26]  A. Varshavsky,et al.  Split ubiquitin as a sensor of protein interactions in vivo. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[27]  P. Walter,et al.  Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes , 1993, The Journal of cell biology.

[28]  D. Shields,et al.  Translocation of preproinsulin across the endoplasmic reticulum membrane. The relationship between nascent polypeptide size and extent of signal recognition particle-mediated inhibition of protein synthesis. , 1992, The Journal of biological chemistry.

[29]  C. Mikoryak,et al.  Turnover of the transferrin receptor is not influenced by removing most of the extracellular domain. , 1991, The Journal of biological chemistry.

[30]  P. Rapiejko,et al.  Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor , 1991, Science.

[31]  J. Hare,et al.  Mechanisms of membrane protein turnover. , 1990, Biochimica et biophysica acta.

[32]  P. Walter,et al.  Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate , 1989, The Journal of cell biology.

[33]  P. Walter,et al.  Ribosome pausing and stacking during translation of a eukaryotic mRNA. , 1988, The EMBO journal.

[34]  Reinhart Heinrich,et al.  Mathematical modeling of the effects of the signal recognition particle on translation and translocation of proteins across the endoplasmic reticulum membrane. , 1987, Journal of molecular biology.

[35]  B. Dobberstein,et al.  Signal recognition particle arrests elongation of nascent secretory and membrane proteins at multiple sites in a transient manner. , 1987, The Journal of biological chemistry.

[36]  T. Rapoport,et al.  Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking , 1987, The Journal of cell biology.

[37]  T. Connolly,et al.  Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein , 1986, The Journal of cell biology.

[38]  Peter Walter,et al.  Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact , 1986, Nature.

[39]  P. Walter,et al.  Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane , 1985, The Journal of cell biology.

[40]  G. Blobel,et al.  Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle , 1982, The Journal of cell biology.

[41]  B. Dobberstein,et al.  Secretory protein translocation across membranes—the role of the ‘docking protein’ , 1982, Nature.

[42]  G. Blobel,et al.  Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site- specific arrest of chain elongation that is released by microsomal membranes , 1981, The Journal of cell biology.

[43]  Oliver Weichenrieder,et al.  Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain. , 2004, Nucleic acids research.

[44]  R. Stroud,et al.  The signal recognition particle. , 2001, Annual review of biochemistry.

[45]  S. Ryser,et al.  The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog. , 1997, Nucleic acids research.