Structure and assembly of the Alu domain of the mammalian signal recognition particle

Nature

Volumn 408, Issue 6809, 2000, Pages 167-173

  Weichenrieder, Oliver ^a   Wild, Klemens ^a   Strub, Katharina ^b   Cusack, Stephen ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^b UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

RNA; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENDOPLASMIC RETICULUM; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN STRUCTURE; RNA TRANSLATION; TRANSLATION REGULATION;

ALU ELEMENTS; ANIMALS; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; RNA; RNA-BINDING PROTEINS; SIGNAL RECOGNITION PARTICLE;

MAMMALIA;

EID: 0034626729     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35041507     Document Type: Article

References (48)

1. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum
2. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
3. Signal recognition particle (SRP), a ubiquitous initiator of protein translocation
4. The organization of the 7SL RNA in the signal recognition particle
5. Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact
6. 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
7. Elongation arrest is a physiologically important function of signal recognition particle
8. Mathematical modeling of the effects of the signal recognition particle on translation and translocation of proteins across the endoplasmic reticulum membrane
9. Secondary structure of the nascent 7S L RNA mediates efficient transcription by RNA polymerase III
10. Accurate 3' end processing and adenylation of human signal recognition particle RNA and Alu RNA in vitro
11. Localization of signal recognition particle RNA in the nucleolus of mammalian cells
12. The DNA sequence of human chromosome 22
13. Nonviral retroposons: Genes, pseudogenes, and transposable elements generated by the reverse flow of genetic information
14. Mobile elements and disease
15. The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs
16. Monomeric scAlu and nascent dimeric Alu RNAs induced by adenovirus are assembled into SRP9/14-containing RNPs in HeLa cells
17. The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog
18. Heterodimer SRP9/14 is an integral part of the neural BC200 RNP in primate brain
19. The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14
20. Identification of a minimal Alu RNA folding domain that specifically binds SRP9/14
21. 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
22. Small is beautiful: Protein micro-crystallography
23. Three-dimensional structure of a hammerhead ribozyme
24. The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
25. A detailed view of a ribosomal active site: The structure of the L11-RNA complex
26. Crystal structure of a conserved ribosomal protein-RNA complex
27. Assembly of the Alu domain of the signal recognition particle (SRP): Dimerization of the two protein components is required for efficient binding to SRP RNA
28. Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: Analysis of biochemical mutants of SRP
29. Comparative analysis of tertiary structure elements in signal recognition particle RNA
30. A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14
31. Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactions
32. Evidence for an extended 7SL RNA structure in the signal recognition particle
33. Bacillus subtilis histone-like protein, HBsu, is an integral component of a SRP-like particle that can bind the Alu domain of small cytoplasmic RNA
34. The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure
35. Binding sites of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined in protein-RNA 'footprinting'
36. Alu sequences
37. AMoRe: An automated package for molecular replacement
38. Crystallography and NMR system: A new software suite for macromolecular structure determination
39. Automated protein model building combined with iterative structure refinement
40. Improved methods for building protein models in electron density maps and the location of errors in these models
41. Processing of X-ray diffraction data collected in oscillation mode
42. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
43. Methods used in the structure determination of bovine mitochondrial F1 ATPase
44. RIBBONS 2.0
45. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
46. Raster3D: Photorealistic molecular graphics
47. Protein folding and association: Insight from the interfacial and thermodynamic properties of hydrocarbon