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Global profiling of SRP interaction with nascent polypeptides
Univ Heidelberg ZMBH, Ctr Mol Biol, DKFZ ZMBH Alliance, Neuenheimer Feld 282, D-69120 Heidelberg, Germany.;German Canc Res Ctr, Neuenheimer Feld 280, D-69120 Heidelberg, Germany..
Univ Heidelberg ZMBH, Ctr Mol Biol, DKFZ ZMBH Alliance, Neuenheimer Feld 282, D-69120 Heidelberg, Germany.;German Canc Res Ctr, Neuenheimer Feld 280, D-69120 Heidelberg, Germany..
HITS gGmbH, Heidelberg Inst Theoret Studies, Schloss Wolfsbrunnenweg 35, D-69118 Heidelberg, Germany..
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi. Stockholm Univ, Ctr Biomembrane Res, Dept Biochem & Biophys, S-10691 Stockholm, Sweden.;Stockholm Univ, Sci Life Lab, S-17121 Solna, Sweden..
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2016 (engelsk)Inngår i: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 536, nr 7615, s. 219-223Artikkel i tidsskrift, Letter (Fagfellevurdert) Published
Abstract [en]

Signal recognition particle (SRP) is a universally conserved protein-RNA complex that mediates co-translational protein translocation and membrane insertion by targeting translating ribosomes to membrane translocons(1). The existence of parallel co- and post-translational transport pathways(2), however, raises the question of the cellular substrate pool of SRP and the molecular basis of substrate selection. Here we determine the binding sites of bacterial SRP within the nascent proteome of Escherichia coli at amino acid resolution, by sequencing messenger RNA footprints of ribosome-nascent-chain complexes associated with SRP. SRP, on the basis of its strong preference for hydrophobic transmembrane domains (TMDs), constitutes a compartment-specific targeting factor for nascent inner membrane proteins (IMPs) that efficiently excludes signal-sequence-containing precursors of periplasmic and outer membrane proteins. SRP associates with hydrophobic TMDs enriched in consecutive stretches of hydrophobic and bulky aromatic amino acids immediately on their emergence from the ribosomal exit tunnel. By contrast with current models, N-terminal TMDs are frequently skipped and TMDs internal to the polypeptide sequence are selectively recognized. Furthermore, SRP binds several TMDs in many multi-spanning membrane proteins, suggesting cycles of SRP-mediated membrane targeting. SRP-mediated targeting is not accompanied by a transient slowdown of translation and is not influenced by the ribosome-associated chaperone trigger factor (TF), which has a distinct substrate pool and acts at different stages during translation. Overall, our proteome-wide data set of SRP-binding sites reveals the underlying principles of pathway decisions for nascent chains in bacteria, with SRP acting as the dominant triaging factor, sufficient to separate IMPs from substrates of the SecA-SecB post-translational translocation and TF-assisted cytosolic protein folding pathways.

sted, utgiver, år, opplag, sider
2016. Vol. 536, nr 7615, s. 219-223
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Identifikatorer
URN: urn:nbn:se:uu:diva-304216DOI: 10.1038/nature19070ISI: 000381472100038PubMedID: 27487212OAI: oai:DiVA.org:uu-304216DiVA, id: diva2:1034842
Forskningsfinansiär
Swedish Research CouncilGerman Research Foundation (DFG), SFB638; FOR1805Tilgjengelig fra: 2016-10-13 Laget: 2016-10-03 Sist oppdatert: 2017-11-29bibliografisk kontrollert

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