Literature DB >> 15168609

The archaeal signal recognition particle: steps toward membrane binding.

Ralf G Moll1.   

Abstract

Signal recognition particles and their receptors target ribosome nascent chain complexes of preproteins toward the protein translocation apparatus of the cell. The discovery of essential SRP components in the third urkingdom of the phylogenetic tree, the archaea (Woese, C. R., and Fox, G. E. (1977). Proc. Natl. Acad. Sci. U.S.A. 74, 5088-5090) raises questions concerning the structure and composition of the archaeal signal recognition particle as well as the functions that route nascent prepoly peptide chains to the membrane. Investigations of the archaeal SRP pathway could therefore identify novel aspects of this process not previously reported or unique to archaea when compared with the respective eukaryal and bacterial systems.

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Year:  2004        PMID: 15168609     DOI: 10.1023/b:jobb.0000019597.36170.5f

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN: 0145-479X            Impact factor:   2.945


  62 in total

1.  Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA.

Authors:  A Prinz; C Behrens; T A Rapoport; E Hartmann; K U Kalies
Journal:  EMBO J       Date:  2000-04-17       Impact factor: 11.598

Review 2.  The signal recognition particle of Archaea.

Authors:  J Eichler; R Moll
Journal:  Trends Microbiol       Date:  2001-03       Impact factor: 17.079

3.  Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway.

Authors:  R Wesley Rose; Thomas Brüser; Jessica C Kissinger; Mechthild Pohlschröder
Journal:  Mol Microbiol       Date:  2002-08       Impact factor: 3.501

4.  Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey.

Authors:  Kieran Dilks; R Wesley Rose; Enno Hartmann; Mechthild Pohlschröder
Journal:  J Bacteriol       Date:  2003-02       Impact factor: 3.490

5.  The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain.

Authors:  C Moser; O Mol; R S Goody; I Sinning
Journal:  Proc Natl Acad Sci U S A       Date:  1997-10-14       Impact factor: 11.205

Review 6.  Protein translocation in the three domains of life: variations on a theme.

Authors:  M Pohlschröder; W A Prinz; E Hartmann; J Beckwith
Journal:  Cell       Date:  1997-11-28       Impact factor: 41.582

7.  The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.

Authors:  N D Ulbrandt; J A Newitt; H D Bernstein
Journal:  Cell       Date:  1997-01-24       Impact factor: 41.582

8.  Ffh and FtsY in a Mycoplasma mycoides signal-recognition particle pathway: SRP RNA and M domain of Ffh are not required for stimulation of GTPase activity in vitro.

Authors:  B Macao; J Luirink; T Samuelsson
Journal:  Mol Microbiol       Date:  1997-05       Impact factor: 3.501

9.  FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins.

Authors:  A Seluanov; E Bibi
Journal:  J Biol Chem       Date:  1997-01-24       Impact factor: 5.157

10.  Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.

Authors:  R Moll; S Schmidtke; G Schäfer
Journal:  Eur J Biochem       Date:  1999-01
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  3 in total

Review 1.  Extreme secretion: protein translocation across the archael plasma membrane.

Authors:  Gabriela Ring; Jerry Eichler
Journal:  J Bioenerg Biomembr       Date:  2004-02       Impact factor: 2.945

Review 2.  Posttranslational protein modification in Archaea.

Authors:  Jerry Eichler; Michael W W Adams
Journal:  Microbiol Mol Biol Rev       Date:  2005-09       Impact factor: 11.056

Review 3.  Archaea signal recognition particle shows the way.

Authors:  Christian Zwieb; Shakhawat Bhuiyan
Journal:  Archaea       Date:  2010-06-28       Impact factor: 3.273

  3 in total

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