Elongation arrest is a physiologically important function of signal recognition particle (Q27931328)

1 December 2016

title

Elongation arrest is a physiologically important function of signal recognition particle (English)

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RNA-binding signal recognition particle subunit SRP54 YPR088C

1 December 2016

main subject

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RNA-binding signal recognition particle subunit SEC65 YML105C

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Signal recognition particle subunit SRP68 YPL243W

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Signal recognition particle subunit SRP21 YKL122C

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RNA-binding signal recognition particle subunit SRP14 YDL092W

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Signal recognition particle subunit SRP72 YPL210C

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author name string

N Mason

series ordinal

1

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L F Ciufo

series ordinal

2

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J D Brown

series ordinal

3

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publication date

1 August 2000

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language of work or name

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describes a project that uses

1 December 2016

volume

19

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issue

15

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page(s)

4164-74

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ImageQuant

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC306590/fullTextXML

inferred from PubMed Central ID database lookup

cites work

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Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression

20 March 2017

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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

20 March 2017

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20 March 2017

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Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum

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Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae

20 March 2017

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The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19

20 March 2017

1 reference

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SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity

20 March 2017

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Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum

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A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins

20 March 2017

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New insights into signal recognition and elongation arrest activities of the signal recognition particle

20 March 2017

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The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14.

29 September 2017

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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

29 September 2017

1 reference

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A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14

29 September 2017

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Signal sequences specify the targeting route to the endoplasmic reticulum membrane

29 September 2017

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ER membrane protein complex required for nuclear fusion

29 September 2017

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Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

29 September 2017

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Ubiquitin-assisted dissection of protein transport across membranes.

29 September 2017

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Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane

29 September 2017

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Signal recognition particle (SRP), a ubiquitous initiator of protein translocation

29 September 2017

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Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes

29 September 2017

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Structure of the signal recognition particle by electron microscopy

29 September 2017

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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

29 September 2017

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The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length

29 September 2017

1 reference

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Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle

29 September 2017

1 reference

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Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=306590

Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=306590

The most abundant small cytoplasmic RNA of Saccharomyces cerevisiae has an important function required for normal cell growth

29 September 2017

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Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=306590

Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=306590

Random mutagenesis of Schizosaccharomyces pombe SRP RNA: lethal and conditional lesions cluster in presumptive protein binding sites

29 September 2017

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Comparative analysis of tertiary structure elements in signal recognition particle RNA.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=306590

Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=306590

SRP samples nascent chains for the presenceof signal sequences by interacting with ribosomes at a discrete step during translation elongation

2 June 2018

1 reference

https://api.crossref.org/works/10.1093%2FEMBOJ%2F19.15.4164

The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FEMBOJ%2F19.15.4164

The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FEMBOJ%2F19.15.4164

Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FEMBOJ%2F19.15.4164

Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal‐recognition particle

21 January 2018

1 reference

12 December 2020

Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation

1 reference

12 December 2020

In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor

1 reference

12 December 2020

Changes in a mammalian signal sequence required for efficient protein secretion by yeasts

1 reference

12 December 2020

Identifiers

DOI

10.1093/EMBOJ/19.15.4164

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