Literature DB >> 27900448

The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.

Sayandeep Gupta1, Mousam Roy1, Abhrajyoti Ghosh2.   

Abstract

The signal recognition particle (SRP) and its receptor constitute universally conserved and essential cellular machinery that controls the proper membrane localization of nascent polypeptides with the transmembrane domain. In the past decade, there has been an immense advancement in our understanding of this targeting machine in all three domains of life. A significant portion of such progress came from the structural analysis of archaeal SRP components. Despite the availability of structural insights from different archaeal SRP components, little is known about protein translocation in this domain of life compared to either bacteria or eukaryotes. One of the primary reasons being limited availability of the genetic and cell biological tools in archaea. In the present review, an attempt has been made to explore the structural information available for archaeal SRP components to gain insights into the protein translocation mechanism of this group of organisms. Besides, many exciting avenues of archaeal research possible using the recently developed genetic and cell biological tools for some species have been identified.

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Year:  2016        PMID: 27900448     DOI: 10.1007/s00284-016-1167-9

Source DB:  PubMed          Journal:  Curr Microbiol        ISSN: 0343-8651            Impact factor:   2.188


  110 in total

1.  Evidence for post-translational membrane insertion of the integral membrane protein bacterioopsin expressed in the heterologous halophilic archaeon Haloferax volcanii.

Authors:  R Ortenberg; M Mevarech
Journal:  J Biol Chem       Date:  2000-07-28       Impact factor: 5.157

Review 2.  SRP-mediated protein targeting: structure and function revisited.

Authors:  Joen Luirink; Irmgard Sinning
Journal:  Biochim Biophys Acta       Date:  2004-11-11

3.  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

4.  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

5.  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

6.  Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains.

Authors:  K Römisch; J Webb; J Herz; S Prehn; R Frank; M Vingron; B Dobberstein
Journal:  Nature       Date:  1989-08-10       Impact factor: 49.962

7.  Evolutionary advantages of polyploidy in halophilic archaea.

Authors:  Jörg Soppa
Journal:  Biochem Soc Trans       Date:  2013-02-01       Impact factor: 5.407

8.  Versatile Genetic Tool Box for the Crenarchaeote Sulfolobus acidocaldarius.

Authors:  Michaela Wagner; Marleen van Wolferen; Alexander Wagner; Kerstin Lassak; Benjamin H Meyer; Julia Reimann; Sonja-Verena Albers
Journal:  Front Microbiol       Date:  2012-06-13       Impact factor: 5.640

9.  A. fulgidus SRP54 M-domain.

Authors:  Udayar Ilangovan; Shakhawat H Bhuiyan; Cynthia S Hinck; Jeffrey T Hoyle; Olga N Pakhomova; Christian Zwieb; Andrew P Hinck
Journal:  J Biomol NMR       Date:  2008-07-11       Impact factor: 2.582

10.  Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.

Authors:  Kaoru Kumazaki; Toshiki Kishimoto; Arata Furukawa; Hiroyuki Mori; Yoshiki Tanaka; Naoshi Dohmae; Ryuichiro Ishitani; Tomoya Tsukazaki; Osamu Nureki
Journal:  Sci Rep       Date:  2014-12-03       Impact factor: 4.379

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  1 in total

1.  RNA antitoxin SprF1 binds ribosomes to attenuate translation and promote persister cell formation in Staphylococcus aureus.

Authors:  Marie-Laure Pinel-Marie; Régine Brielle; Camille Riffaud; Noëlla Germain-Amiot; Norbert Polacek; Brice Felden
Journal:  Nat Microbiol       Date:  2021-01-04       Impact factor: 17.745

  1 in total

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