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Literature DB >> 3856232

Structure of the signal recognition particle by electron microscopy.

Abstract

The signal recognition particle (SRP) is a ribonucleoprotein consisting of six distinct polypeptide components and one molecule of small cytoplasmic RNA (7SL RNA). The particle was previously shown to function in protein translocation across and protein integration into the endoplasmic reticulum membrane. Homogeneous signal recognition particle preparations were visualized by electron microscopy (i) after negative staining, (ii) by dark-field imaging of unstained specimens, and (iii) by platinum-shadowing. The results of each of these different techniques indicate that the signal recognition particle is a rod-shaped particle 5-6 nm wide and 23-24 nm long.

Entities: Chemical

Mesh：

Substances：

Year: 1985 PMID： 3856232 PMCID： PMC397131 DOI： 10.1073/pnas.82.3.785

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

17 in total

1. Heavy atoms in model compounds and nucleic acid imaged by dark field transmission electron microscopy.

Authors: R F Whiting; F P Ottensmeyer
Journal: J Mol Biol Date: 1972-06-20 Impact factor: 5.469

2. Protein translocation across the endoplasmic reticulum.

Authors: P Walter; R Gilmore; G Blobel
Journal: Cell Date: 1984-08 Impact factor: 41.582

3. A model for the structure of nucleoprotamine.

Authors: D P Bazett-Jones; F P Ottensmeyer
Journal: J Ultrastruct Res Date: 1979-06

4. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum.

Authors: P Walter; G Blobel
Journal: Nature Date: 1982-10-21 Impact factor: 49.962

5. Ribosomal proteins L1, L17 and L27 from Escherichia coli localized at single sites on the large subunit by immune electron microscopy.

Authors: J A Lake; W A Strycharz
Journal: J Mol Biol Date: 1981-12-25 Impact factor: 5.469

6. Secretory protein translocation across membranes-the role of the "docking protein'.

Authors: D I Meyer; E Krause; B Dobberstein
Journal: Nature Date: 1982-06-24 Impact factor: 49.962

7. Structure analysis of small proteins by electron microscopy: valinomycin, bacitracin and low molecular weight cell growth stimulators.

Authors: F P Ottensmeyer; D P Bazett-Jones; J Hewitt; G B Price
Journal: Ultramicroscopy Date: 1978 Impact factor: 2.689

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

Authors: P Walter; G Blobel
Journal: Proc Natl Acad Sci U S A Date: 1980-12 Impact factor: 11.205

9. 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.

Authors: P Walter; G Blobel
Journal: J Cell Biol Date: 1981-11 Impact factor: 10.539

10. Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.

Authors: P Walter; I Ibrahimi; G Blobel
Journal: J Cell Biol Date: 1981-11 Impact factor: 10.539

9 in total

4. Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined in protein-RNA "footprinting".

Authors: V Siegel; P Walter
Journal: Proc Natl Acad Sci U S A Date: 1988-03 Impact factor: 11.205

Structure of the signal recognition particle by electron microscopy.

1. Heavy atoms in model compounds and nucleic acid imaged by dark field transmission electron microscopy.

2. Protein translocation across the endoplasmic reticulum.

3. A model for the structure of nucleoprotamine.

4. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum.

5. Ribosomal proteins L1, L17 and L27 from Escherichia coli localized at single sites on the large subunit by immune electron microscopy.

6. Secretory protein translocation across membranes-the role of the "docking protein'.

7. Structure analysis of small proteins by electron microscopy: valinomycin, bacitracin and low molecular weight cell growth stimulators.

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

9. 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.

10. Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.

1. Hierarchical assembly of the Alu domain of the mammalian signal recognition particle.

2. The structure of Escherichia coli signal recognition particle revealed by scanning transmission electron microscopy.

3. The secondary structure of the 7SL RNA in the signal recognition particle: functional implications.

4. Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined in protein-RNA "footprinting".

5. Diversity of 7 SL RNA from the signal recognition particle of maize endosperm.

6. Elongation arrest is a physiologically important function of signal recognition particle.

7. Evidence for an extended 7SL RNA structure in the signal recognition particle.

8. Changes in 7SL RNA conformation during the signal recognition particle cycle.

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