Literature DB >> 15189152

Structural insights into the signal recognition particle.

Jennifer A Doudna1, Robert T Batey.   

Abstract

The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway.

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Year:  2004        PMID： 15189152     DOI： 10.1146/annurev.biochem.73.011303.074048

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN： 0066-4154            Impact factor:   23.643


  61 in total

1.  Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.

Authors:  Laurent Huck; Anne Scherrer; Lionel Terzi; Arthur E Johnson; Harris D Bernstein; Stephen Cusack; Oliver Weichenrieder; Katharina Strub
Journal:  Nucleic Acids Res       Date:  2004-09-21       Impact factor: 16.971

Review 2.  Roles of DEAD-box proteins in RNA and RNP Folding.

Authors:  Cynthia Pan; Rick Russell
Journal:  RNA Biol       Date:  2010-11-01       Impact factor: 4.652

3.  Transient Protein-RNA Interactions Guide Nascent Ribosomal RNA Folding.

Authors:  Olivier Duss; Galina A Stepanyuk; Joseph D Puglisi; James R Williamson
Journal:  Cell       Date:  2019-11-21       Impact factor: 41.582

4.  Structural insights into SRP RNA: an induced fit mechanism for SRP assembly.

Authors:  Tobias Hainzl; Shenghua Huang; A Elisabeth Sauer-Eriksson
Journal:  RNA       Date:  2005-05-31       Impact factor: 4.942

5.  Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY.

Authors:  Iwona Buskiewicz; Andriy Kubarenko; Frank Peske; Marina V Rodnina; Wolfgang Wintermeyer
Journal:  RNA       Date:  2005-06       Impact factor: 4.942

6.  Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site.

Authors:  Pamela J Focia; Joseph Gawronski-Salerno; John S Coon; Douglas M Freymann
Journal:  J Mol Biol       Date:  2006-05-26       Impact factor: 5.469

7.  Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.

Authors:  Thomas U Schwartz; Daniel Schmidt; Stephen G Brohawn; Günter Blobel
Journal:  Proc Natl Acad Sci U S A       Date:  2006-04-20       Impact factor: 11.205

8.  The structural basis of FtsY recruitment and GTPase activation by SRP RNA.

Authors:  Felix Voigts-Hoffmann; Nikolaus Schmitz; Kuang Shen; Shu-Ou Shan; Sandro F Ataide; Nenad Ban
Journal:  Mol Cell       Date:  2013-11-07       Impact factor: 17.970

Review 9.  The structural and functional diversity of metabolite-binding riboswitches.

Authors:  Adam Roth; Ronald R Breaker
Journal:  Annu Rev Biochem       Date:  2009       Impact factor: 23.643

10.  Anti-cooperative assembly of the SRP19 and SRP68/72 components of the signal recognition particle.

Authors:  Tuhin Subhra Maity; Howard M Fried; Kevin M Weeks
Journal:  Biochem J       Date:  2008-11-01       Impact factor: 3.857
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