Literature DB >> 10195420

New insights into signal recognition and elongation arrest activities of the signal recognition particle.

N Bui1, K Strub.   

Abstract

The signal recognition particle (SRP), a ubiquitous cytoplasmic ribonucleoprotein particle, plays an essential role in promoting co-translational translocation of proteins into the endoplasmic reticulum. Here, we summarise recent progress made in the understanding of two essential SRP functions: the signal recognition function, which ensures the specificity, and the elongation arrest function, which increases the efficiency of translocation. Our discussion is based on functional data as well as on atomic structure information, both of which also support the notion that SRP is a very ancient particle closely related to ribosomes. Based on the significant increase of knowledge that has been accumulating on the structure of elongation factors and on their interactions with the ribosome, we speculate about a possible mechanism of the elongation arrest function.

Mesh:

Substances:

Year:  1999        PMID: 10195420     DOI: 10.1515/BC.1999.021

Source DB:  PubMed          Journal:  Biol Chem        ISSN: 1431-6730            Impact factor:   3.915


  15 in total

1.  SRPDB (signal recognition particle database).

Authors:  C Zwieb; T Samuelsson
Journal:  Nucleic Acids Res       Date:  2000-01-01       Impact factor: 16.971

2.  SRPDB (Signal Recognition Particle Database).

Authors:  J Gorodkin; B Knudsen; C Zwieb; T Samuelsson
Journal:  Nucleic Acids Res       Date:  2001-01-01       Impact factor: 16.971

3.  Signal recognition particle components in the nucleolus.

Authors:  J C Politz; S Yarovoi; S M Kilroy; K Gowda; C Zwieb; T Pederson
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-04       Impact factor: 11.205

4.  Assembly of the human signal recognition particle (SRP): overlap of regions required for binding of protein SRP54 and assembly control.

Authors:  J Yin; C H Yang; C Zwieb
Journal:  RNA       Date:  2001-10       Impact factor: 4.942

5.  Assembly of archaeal signal recognition particle from recombinant components.

Authors:  S H Bhuiyan; K Gowda; H Hotokezaka; C Zwieb
Journal:  Nucleic Acids Res       Date:  2000-03-15       Impact factor: 16.971

6.  Conformation of 4.5S RNA in the signal recognition particle and on the 30S ribosomal subunit.

Authors:  Shan-Qing Gu; Johannes Jöckel; Philipp Beinker; Jens Warnecke; Yuri P Semenkov; Marina V Rodnina; Wolfgang Wintermeyer
Journal:  RNA       Date:  2005-07-25       Impact factor: 4.942

7.  Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain.

Authors:  Rob W Van Nues; Jeremy D Brown
Journal:  RNA       Date:  2004-01       Impact factor: 4.942

8.  Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli.

Authors:  Christina Wilson Bowers; Fion Lau; Thomas J Silhavy
Journal:  J Bacteriol       Date:  2003-10       Impact factor: 3.490

9.  Inhibitors of MAPK pathway ERK1/2 or p38 prevent the IL-1{beta}-induced up-regulation of SRP72 autoantigen in Jurkat cells.

Authors:  Victor E Arana-Argáez; Vidal Delgado-Rizo; Oscar E Pizano-Martínez; Erika A Martínez-Garcia; Beatriz T Martín-Márquez; Andrea Muñoz-Gómez; Marcelo H Petri; Juan Armendáriz-Borunda; Guillermo Espinosa-Ramírez; Diego A Zúñiga-Tamayo; Rafael Herrera-Esparza; Mónica Vázquez-Del Mercado
Journal:  J Biol Chem       Date:  2010-08-19       Impact factor: 5.157

10.  Escherichia coli SRP, its protein subunit Ffh, and the Ffh M domain are able to selectively limit membrane protein expression when overexpressed.

Authors:  Ido Yosef; Elena S Bochkareva; Eitan Bibi
Journal:  mBio       Date:  2010-06-08       Impact factor: 7.867

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.