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The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective

Overview
Journal Curr Microbiol
Specialty Microbiology
Date 2016 Dec 1
PMID 27900448
Citations 1
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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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References
1.
Romisch K, Webb J, Herz J, Prehn S, Frank R, Vingron M . Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Nature. 1989; 340(6233):478-82. DOI: 10.1038/340478a0. View

2.
Moser C, Mol O, Goody R, Sinning I . The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain. Proc Natl Acad Sci U S A. 1997; 94(21):11339-44. PMC: 23460. DOI: 10.1073/pnas.94.21.11339. View

3.
Ortenberg R, Mevarech M . Evidence for post-translational membrane insertion of the integral membrane protein bacterioopsin expressed in the heterologous halophilic archaeon Haloferax volcanii. J Biol Chem. 2000; 275(30):22839-46. DOI: 10.1074/jbc.M908916199. View

4.
Kumazaki K, Kishimoto T, Furukawa A, Mori H, Tanaka Y, Dohmae N . Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase. Sci Rep. 2014; 4:7299. PMC: 4252904. DOI: 10.1038/srep07299. View

5.
Luirink J, Sinning I . SRP-mediated protein targeting: structure and function revisited. Biochim Biophys Acta. 2004; 1694(1-3):17-35. DOI: 10.1016/j.bbamcr.2004.03.013. View