Journal ArticleDOI
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
Mario Halic,Thomas Becker,Martin R. Pool,Christian M. T. Spahn,Robert A. Grassucci,Robert A. Grassucci,Joachim Frank,Joachim Frank,Roland Beckmann +8 more
TLDR
The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.Abstract:
Cotranslational translocation of proteins across or into membranes is a vital process in all kingdoms of life. It requires that the translating ribosome be targeted to the membrane by the signal recognition particle (SRP), an evolutionarily conserved ribonucleoprotein particle. SRP recognizes signal sequences of nascent protein chains emerging from the ribosome. Subsequent binding of SRP leads to a pause in peptide elongation and to the ribosome docking to the membrane-bound SRP receptor. Here we present the structure of a targeting complex consisting of mammalian SRP bound to an active 80S ribosome carrying a signal sequence. This structure, solved to 12 A by cryo-electron microscopy, enables us to generate a molecular model of SRP in its functional conformation. The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.read more
Citations
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Journal ArticleDOI
Structures of the bacterial ribosome at 3.5 Å resolution
Barbara S Schuwirth,Maria A. Borovinskaya,Cathy W Hau,Wen Zhang,Antón Vila-Sanjurjo,James M. Holton,Jamie H. D. Cate,Jamie H. D. Cate +7 more
TL;DR: Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA and transfer RNAs during translocation.
Journal ArticleDOI
RNA in unexpected places: long non-coding RNA functions in diverse cellular contexts
Sarah Geisler,Jeff Coller +1 more
TL;DR: A paradigm in which lncRNAs regulate transcription via chromatin modulation is supported, but new functions are steadily emerging, including post-transcriptional regulation, organization of protein complexes, cell-cell signalling and allosteric regulation of proteins.
Journal ArticleDOI
The Structure of the Eukaryotic Ribosome at 3.0 Å Resolution
Adam Ben-Shem,Nicolas Garreau de Loubresse,Sergey Melnikov,Lasse Jenner,Gulnara Yusupova,Marat Yusupov +5 more
TL;DR: The crystal structure of the 80S ribosome from the yeast Saccharomyces cerevisiae is reported, which reveals the architecture of eukaryote-specific elements and their interaction with the universally conserved core, and describes all eukariotes-specific bridges between the two ribosomal subunits.
Journal ArticleDOI
The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
TL;DR: The early co-translational events involving the ribosome that guide cytosolic proteins to their native state are reviewed.
Journal ArticleDOI
Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
TL;DR: A cytosolic TMD recognition complex (TRC) that targets TA proteins for insertion into the ER membrane, and an ATPase-deficient mutant of TRC40/Asna-1 dominantly inhibited TA protein insertion selectively without influencing other translocation pathways.
References
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Journal ArticleDOI
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.
Peter Walter,Gonter Blobel +1 more
TL;DR: It is concluded that the interaction of SRP with the amino-terminal signal peptide of the nascent chain (emerged from the large ribosomal subunit) that modulates translation and thereby causes an arrest in chain elongation.