Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii

Irit Tozik, Qiaojia Huang, Christian W Zwieb, Jerry Eichler

Research output: Contribution to journalArticle

32 Citations (Scopus)

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 eukeryal 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.

Original languageEnglish (US)
Pages (from-to)4166-4175
Number of pages10
JournalNucleic Acids Research
Volume30
Issue number19
StatePublished - Oct 1 2002
Externally publishedYes

Fingerprint

Haloferax volcanii
Signal Recognition Particle
Archaea
Ribonucleoproteins
Salts
RNA
Protein Subunits
Amino Acid Sequence

ASJC Scopus subject areas

  • Genetics

Cite this

Tozik, I., Huang, Q., Zwieb, C. W., & Eichler, J. (2002). Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii. Nucleic Acids Research, 30(19), 4166-4175.

Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii. / Tozik, Irit; Huang, Qiaojia; Zwieb, Christian W; Eichler, Jerry.

In: Nucleic Acids Research, Vol. 30, No. 19, 01.10.2002, p. 4166-4175.

Research output: Contribution to journalArticle

Tozik, I, Huang, Q, Zwieb, CW & Eichler, J 2002, 'Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii', Nucleic Acids Research, vol. 30, no. 19, pp. 4166-4175.
Tozik, Irit ; Huang, Qiaojia ; Zwieb, Christian W ; Eichler, Jerry. / Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii. In: Nucleic Acids Research. 2002 ; Vol. 30, No. 19. pp. 4166-4175.
@article{293afc02c25441d1b8d2e4b413680b41,
title = "Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii",
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 eukeryal 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.",
author = "Irit Tozik and Qiaojia Huang and Zwieb, {Christian W} and Jerry Eichler",
year = "2002",
month = "10",
day = "1",
language = "English (US)",
volume = "30",
pages = "4166--4175",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "19",

}

TY - JOUR

T1 - Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii

AU - Tozik, Irit

AU - Huang, Qiaojia

AU - Zwieb, Christian W

AU - Eichler, Jerry

PY - 2002/10/1

Y1 - 2002/10/1

N2 - 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 eukeryal 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.

AB - 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 eukeryal 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.

UR - http://www.scopus.com/inward/record.url?scp=0036799450&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036799450&partnerID=8YFLogxK

M3 - Article

C2 - 12364595

AN - SCOPUS:0036799450

VL - 30

SP - 4166

EP - 4175

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 19

ER -