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Titolo:
Hierarchical assembly of the Alu domain of the mammalian signal recognition particle
Autore:
Weichenrieder, O; Stehlin, C; Kapp, U; Birse, DE; Timmins, PA; Strub, K; Cusack, S;
Indirizzi:
European Mol Biol Lab, Grenoble Outstn, F-38042 Grenoble 9, France European Mol Biol Lab Grenoble France 9 tstn, F-38042 Grenoble 9, France Inst Max Von Laue Paul Langevin, F-38042 Grenoble, France Inst Max Von Laue Paul Langevin Grenoble France F-38042 Grenoble, France Univ Geneva, Dept Biol Cellulaire, CH-1211 Geneva 4, Switzerland Univ Geneva Geneva Switzerland 4 llulaire, CH-1211 Geneva 4, Switzerland
Titolo Testata:
RNA-A PUBLICATION OF THE RNA SOCIETY
fascicolo: 5, volume: 7, anno: 2001,
pagine: 731 - 740
SICI:
1355-8382(200105)7:5<731:HAOTAD>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; SRP-RNA; BINDING-SITES; PROTEIN TRANSLOCATION; ENDOPLASMIC-RETICULUM; 4.5S RNA; 7SL RNA; COMPONENTS; SRP9/14; RIBONUCLEOPROTEIN;
Keywords:
retroposition; RNA-protein recognition; RNP assembly; signal recognition particle; translational control;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Cusack, S European Mol Biol Lab, Grenoble Outstn, BP 156X, F-38042 Grenoble 9, France European Mol Biol Lab BP 156X Grenoble France 9 noble 9, France
Citazione:
O. Weichenrieder et al., "Hierarchical assembly of the Alu domain of the mammalian signal recognition particle", RNA, 7(5), 2001, pp. 731-740

Abstract

The mammalian signal recognition particle (SRP) catalytically promotes cotranslational translocation of signal sequence containing proteins across the endoplasmic reticulum membrane. While the S-domain of SRP binds the N-terminal signal sequence on the nascent polypeptide, the Alu domain of SRP temporarily interferes with the ribosomal elongation cycle until the translocation pore in the membrane is correctly engaged. Here we present biochemicaland biophysical evidence for a hierarchical assembly pathway of the SRP Alu domain. The proteins SRP9 and SRP14 first heterodimerize and then initially bind to the Alu RNA 5' domain. This creates the binding site for the AluRNA 3' domain. Alu RNA then undergoes a large conformational change with the flexibly linked 3' domain folding back by 180 degrees onto the 5' domaincomplex to form the final compact Alu ribonucleoprotein particle (Alu RNP). We discuss the possible mechanistic consequences of the likely reversibility of this final step with reference to translational regulation by the SRP Alu domain and with reference to the structurally similar Alu RNP retroposition intermediates derived from Alu elements in genomic DNA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:44:45