ArticleNucleic acids research2002
Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
- Evolution of the archaeal and mammalian information processing systems: towards an archaeal model for human disease.Cellular and molecular life sciences : CMLS · 2017Review
- AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase.Journal of bacteriology · 2012Article
- Compositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.Journal of molecular evolution · 2011Article
- Archaea signal recognition particle shows the way.Archaea (Vancouver, B.C.) · 2010Review
- Compositional properties and thermal adaptation of SRP-RNA in bacteria and archaea.Journal of molecular evolution · 2010Article
- Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010Review
- Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii.Journal of bacteriology · 2008Article
- The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72.RNA (New York, N.Y.) · 2008Article
- Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein.Journal of bacteriology · 2008Article
- Article
- SRP19 is a dispensable component of the signal recognition particle in Archaea.Journal of bacteriology · 2007Article
- The Haloferax volcanii FtsY homolog is critical for haloarchaeal growth but does not require the A domain.Journal of bacteriology · 2005Article
- The conserved adenosine in helix 6 of Archaeoglobus fulgidus signal recognition particle RNA initiates SRP assembly.Archaea (Vancouver, B.C.) · 2004Article
- The archaeal Sec-dependent protein translocation pathway.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- The archaeal signal recognition particle: steps toward membrane binding.Journal of bioenergetics and biomembranes · 2004Review
- Extreme secretion: protein translocation across the archael plasma membrane.Journal of bioenergetics and biomembranes · 2004Review
- Protein-protein, protein-RNA and protein-lipid interactions of signal-recognition particle components in the hyperthermoacidophilic archaeon Acidianus ambivalens.The Biochemical journal · 2003Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The signal recognition particle (SRP) is a ribonucleoprotein complex involved in the recognition and targeting of nascent extracytoplasmic proteins in all three domains of life. In Archaea, SRP contains 7S RNA like its eukaryal counterpart, yet only includes two of the six protein subunits found in the eukaryal complex. To further our understanding of the archaeal SRP, 7S RNA, SRP19 and SRP54 of the halophilic archaeon Haloferax volcanii have been expressed and purified, and used to reconstitute the ternary SRP complex. The availability of SRP components from a haloarchaeon offers insight into the structure, assembly and function of this ribonucleoprotein complex at saturating salt conditions. While the amino acid sequences of H.volcanii SRP19 and SRP54 are modified presumably as an adaptation to their saline surroundings, the interactions between these halophilic SRP components and SRP RNA appear conserved, with the possibility of a few exceptions. Indeed, the H.volcanii SRP can assemble in the absence of high salt. As reported with other archaeal SRPs, the limited binding of H.volcanii SRP54 to SRP RNA is enhanced in the presence of SRP19. Finally, immunolocalization reveals that H.volcanii SRP54 is found in the cytosolic fraction, where it is associated with the ribosomal fraction of the cell.
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Registered trials
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