Literature DB >> 21336278

Structural basis of signal-sequence recognition by the signal recognition particle.

Tobias Hainzl1, Shenghua Huang, Gitte Meriläinen, Kristoffer Brännström, A Elisabeth Sauer-Eriksson.   

Abstract

The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180° flip of the NG domain-structural changes that ensure a hierarchical succession of events during protein targeting.

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Year:  2011        PMID： 21336278     DOI： 10.1038/nsmb.1994

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN： 1545-9985            Impact factor:   15.369


  18 in total

1.  Crystal structure of the ribonucleoprotein core of the signal recognition particle.

Authors:  R T Batey; R P Rambo; L Lucast; B Rha; J A Doudna
Journal:  Science       Date:  2000-02-18       Impact factor: 47.728

2.  Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY.

Authors:  J R Jagath; N B Matassova; E de Leeuw; J M Warnecke; G Lentzen; M V Rodnina; J Luirink; W Wintermeyer
Journal:  RNA       Date:  2001-02       Impact factor: 4.942

3.  Substrate twinning activates the signal recognition particle and its receptor.

Authors:  Pascal F Egea; Shu-Ou Shan; Johanna Napetschnig; David F Savage; Peter Walter; Robert M Stroud
Journal:  Nature       Date:  2004-01-15       Impact factor: 49.962

4.  Structure of the signal recognition particle interacting with the elongation-arrested ribosome.

Authors:  Mario Halic; Thomas Becker; Martin R Pool; Christian M T Spahn; Robert A Grassucci; Joachim Frank; Roland Beckmann
Journal:  Nature       Date:  2004-02-26       Impact factor: 49.962

Review 5.  Targeting proteins to membranes: structure of the signal recognition particle.

Authors:  Pascal F Egea; Robert M Stroud; Peter Walter
Journal:  Curr Opin Struct Biol       Date:  2005-04       Impact factor: 6.809

6.  Induced structural changes of 7SL RNA during the assembly of human signal recognition particle.

Authors:  Andreas Kuglstatter; Chris Oubridge; Kiyoshi Nagai
Journal:  Nat Struct Biol       Date:  2002-10

7.  Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle.

Authors:  Tobias Hainzl; Shenghua Huang; A Elisabeth Sauer-Eriksson
Journal:  Proc Natl Acad Sci U S A       Date:  2007-09-10       Impact factor: 11.205

8.  Structure of the conserved GTPase domain of the signal recognition particle.

Authors:  D M Freymann; R J Keenan; R M Stroud; P Walter
Journal:  Nature       Date:  1997-01-23       Impact factor: 49.962

9.  Recognition of a signal peptide by the signal recognition particle.

Authors:  Claudia Y Janda; Jade Li; Chris Oubridge; Helena Hernández; Carol V Robinson; Kiyoshi Nagai
Journal:  Nature       Date:  2010-04-04       Impact factor: 49.962

10.  Signal sequences activate the catalytic switch of SRP RNA.

Authors:  Niels Bradshaw; Saskia B Neher; David S Booth; Peter Walter
Journal:  Science       Date:  2009-01-02       Impact factor: 47.728
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  40 in total

Review 1.  Protein export through the bacterial Sec pathway.

Authors:  Alexandra Tsirigotaki; Jozefien De Geyter; Nikolina Šoštaric; Anastassios Economou; Spyridoula Karamanou
Journal:  Nat Rev Microbiol       Date:  2016-11-28       Impact factor: 60.633

2.  Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting.

Authors:  Jae Ho Lee; Sowmya Chandrasekar; SangYoon Chung; Yu-Hsien Hwang Fu; Demi Liu; Shimon Weiss; Shu-Ou Shan
Journal:  Proc Natl Acad Sci U S A       Date:  2018-05-30       Impact factor: 11.205

3.  Dynamic switch of the signal recognition particle from scanning to targeting.

Authors:  Wolf Holtkamp; Sejeong Lee; Thomas Bornemann; Tamara Senyushkina; Marina V Rodnina; Wolfgang Wintermeyer
Journal:  Nat Struct Mol Biol       Date:  2012-11-11       Impact factor: 15.369

4.  Signal recognition particle-ribosome binding is sensitive to nascent chain length.

Authors:  Thomas R Noriega; Albert Tsai; Margaret M Elvekrog; Alexey Petrov; Saskia B Neher; Jin Chen; Niels Bradshaw; Joseph D Puglisi; Peter Walter
Journal:  J Biol Chem       Date:  2014-05-07       Impact factor: 5.157

5.  Allosteric response and substrate sensitivity in peptide binding of the signal recognition particle.

Authors:  Connie Y Wang; Thomas F Miller
Journal:  J Biol Chem       Date:  2014-09-18       Impact factor: 5.157

6.  Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.

Authors:  Rory C Henderson; Feng Gao; Srinivas Jayanthi; Alicia Kight; Priyanka Sharma; Robyn L Goforth; Colin D Heyes; Ralph L Henry; Thallapuranam Krishnaswamy Suresh Kumar
Journal:  Biophys J       Date:  2016-09-20       Impact factor: 4.033

7.  Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.

Authors:  Matthias M M Becker; Karine Lapouge; Bernd Segnitz; Klemens Wild; Irmgard Sinning
Journal:  Nucleic Acids Res       Date:  2016-11-29       Impact factor: 16.971

8.  Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.

Authors:  Eva Pross; Andreas Kuhn
Journal:  J Bacteriol       Date:  2020-12-07       Impact factor: 3.490

Review 9.  "Multiple partial recognitions in dynamic equilibrium" in the binding sites of proteins form the molecular basis of promiscuous recognition of structurally diverse ligands.

Authors:  Daisuke Kohda
Journal:  Biophys Rev       Date:  2017-12-14

10.  A YidC-like Protein in the Archaeal Plasma Membrane.

Authors:  Marta T Borowska; Pawel K Dominik; S Andrei Anghel; Anthony A Kossiakoff; Robert J Keenan
Journal:  Structure       Date:  2015-08-06       Impact factor: 5.006
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