DOI: 10.1093/emboj/19.15.4164. Elongation arrest is a physiologically important function of signal recognition particle

Elongation arrest is a physiologically important function of signal recognition particle

10.1093/emboj/19.15.4164

Crossref journal-article

Springer Science and Business Media LLC

The EMBO Journal (297)

Bibliography

Mason, N., Ciufo, L. F., & Brown, J. D. (2000). Elongation arrest is a physiologically important function of signal recognition particle. The EMBO Journal, 19(15), 4164â4174.

Authors 3

Nicola Mason (first)
Leonora F. Ciufo (additional)
Jeremy D. Brown (additional)

References 41 Referenced 103

10.1073/pnas.82.3.785 / Proc Natl Acad Sci USA / Structure of the signal recognition particle by electron microscopy by Andrews (1985)
10.1093/emboj/16.13.3757 / EMBO J / The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14 by Birse (1997)
10.1002/j.1460-2075.1994.tb06759.x / EMBO J / Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression by Brown (1994)
10.1515/BC.1999.021 / Biol Chem / New insights into signal recognition and elongation arrest activities of the signal recognition particle by Bui (1999)
10.1093/nar/25.6.1117 / Nucleic Acids Res / A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14 by Chang (1997)
10.1128/MCB.9.8.3260 / Mol Cell Biol / The most abundant small cytoplasmic RNA of Saccharomyces cerevisiae has an important function required for normal cell growth by Felici (1989)
10.1016/0092-8674(91)90577-L / Cell / The signal recognition particle in S.cerevisiae by Hann (1991)
10.1038/356532a0 / Nature / SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity by Hann (1992)
10.1083/jcb.106.4.1075 / J Cell Biol / Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae by Hansen (1988)
10.1016/0092-8674(86)90325-9 / Cell / In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α factor by Hansen (1986)
10.1002/j.1460-2075.1995.tb00235.x / EMBO J / A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins by Hauser (1995)
10.1002/j.1460-2075.1994.tb06559.x / EMBO J / Ubiquitin-assisted dissection of protein transport across membranes by Johnsson (1994)
10.1073/pnas.83.22.8604 / Proc Natl Acad Sci USA / Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle by Krieg (1986)
10.1038/320634a0 / Nature / The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle by Kurzchalia (1986)
10.1093/nar/20.7.1607 / Nucleic Acids Res / Random mutagenesis of Schizosaccharomyces pombe SRP RNA: lethal and conditional lesions cluster in presumptive protein binding sites by Liao (1992)
10.1038/359741a0 / Nature / Signal sequence recognition by an Escherichia coli ribonucleoprotein complex by Luirink (1992)
10.1111/j.1432-1033.1995.tb20293.x / Eur J Biochem / Signal recognition particle (SRP), a ubiquitous initiator of protein translocation by Lütcke (1995)
10.1083/jcb.132.4.499 / J Cell Biol / ER membrane protein complex required for nuclear fusion by Ng (1996)
10.1083/jcb.134.2.269 / J Cell Biol / Signal sequences specify the targeting route to the endoplasmic reticulum membrane by Ng (1996)
10.1016/0378-1119(90)90286-Z / Gene / Changes in a mammalian signal sequence required for efficient protein secretion by yeasts by Ngsee (1990)
10.1016/S0092-8674(05)80012-1 / Cell / SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step in translation elongation by Ogg (1995)
10.1091/mbc.3.8.895 / Mol Biol Cell / The signal recognition particle receptor is important for growth and protein secretion in Saccharomyces cerevisiae by Ogg (1992)
10.1016/S0960-9822(02)00484-0 / Curr Biol / The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome by Powers (1996)
10.1046/j.1432-1327.1998.2520016.x / Eur J Biochem / Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle by Rothe (1998)
10.1083/jcb.100.6.1913 / J Cell Biol / Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane by Siegel (1985)
10.1038/320081a0 / Nature / Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact by Siegel (1986)
10.1002/j.1460-2075.1988.tb03007.x / EMBO J / The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length by Siegel (1988a)
10.1016/0092-8674(88)90529-6 / Cell / Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP by Siegel (1988b)
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10.1093/nar/25.10.1920 / Nucleic Acids Res / A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle by Thomas (1997)
10.1002/j.1460-2075.1995.tb00236.x / EMBO J / Early events in preprotein recognition in E.coli: interaction of SRP and trigger factor with nascent polypeptides by Valent (1995)
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10.1083/jcb.109.6.2617 / J Cell Biol / Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate by Wolin (1989)
10.1016/S1359-0278(96)00044-2 / Fold Des / Comparative analysis of tertiary structure elements in signal recognition particle RNA by Zwieb (1996)

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 6:28 p.m.)
Deposited	1 year, 8 months ago (Dec. 18, 2023, 4:06 p.m.)
Indexed	1 month, 2 weeks ago (July 16, 2025, 7:58 a.m.)
Issued	25 years, 1 month ago (Aug. 1, 2000)
Published	25 years, 1 month ago (Aug. 1, 2000)
Published Online	25 years, 1 month ago (Aug. 1, 2000)
Published Print	25 years, 1 month ago (Aug. 1, 2000)

Funders 0

None

BibTeX

@article{Mason_2000, title={Elongation arrest is a physiologically important function of signal recognition particle}, volume={19}, ISSN={0261-4189}, url={http://dx.doi.org/10.1093/emboj/19.15.4164}, DOI={10.1093/emboj/19.15.4164}, number={15}, journal={The EMBO Journal}, publisher={Springer Science and Business Media LLC}, author={Mason, Nicola and Ciufo, Leonora F. and Brown, Jeremy D.}, year={2000}, month=aug, pages={4164–4174} }

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