The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome

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dc.contributor.authorGu, Shan-Qing
dc.contributor.authorPeske, Frank
dc.contributor.authorWieden, Hans-Joachim
dc.contributor.authorRodnina, Marina V.
dc.contributor.authorWintermeyer, Wolfgang
dc.date.accessioned2019-07-17T21:15:31Z
dc.date.available2019-07-17T21:15:31Z
dc.date.issued2003
dc.descriptionSherpa Romeo green journal. Permission to archive final published versionen_US
dc.description.abstractThe signal recognition particle (SRP) from Escherichia coli, composed of Ffh protein and 4.5S RNA, mediates membrane targeting of translating ribosomes displaying a signal or signal-anchor sequence. SRP binds at the peptide exit of the large ribosomal subunit. Structural details of the interaction are not known. Here, the position of Ffh or SRP on the ribosome was probed by using site-specific UV-induced crosslinking by p-azidophenacyl bromide (AzP) attached to a number of cysteine residues engineered into surface positions of Ffh. Efficient crosslinking to vacant ribosomes took place from two positions (AzP17 and AzP25) in the N domain of Ffh, both with Ffh and SRP. Both AzP17 and AzP25 were predominantly crosslinked to ribosomal protein L23 that is located at the peptide exit of the 50S subunit.The SRP receptor, FtsY, did not change the crosslink pattern, whereas the presence of a nascent signal peptide on the ribosome resulted in a second crosslink between Ffh(AzP17) and protein L23, indicating that binding to the nascent signal peptide induced a slightly different arrangement of SRP on the ribosome. These results indicate a model of the topographical arrangement of SRP at the peptide exit of the 50S ribosomal subunit.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationGu, S., Peske, F., Wieden, H. J., Rodnina, M. V., & Wintermeyer, W. (2003). The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome. RNA, 9(5), 566-73. http://www.rnajournal.org/cgi/doi/ 10.1261/rna.2196403.en_US
dc.identifier.urihttps://hdl.handle.net/10133/5469
dc.language.isoen_USen_US
dc.publisherCold Springs Harbor Laboratory Pressen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Witten/Herdeckeen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://dx.doi.org/10.1261/rna.2196403
dc.subject4.5S RNAen_US
dc.subjectMembrane targetingen_US
dc.subjectRibosome nascent chain complexesen_US
dc.subjectSignal peptideen_US
dc.subjectCrosslinking (Polymerization)en_US
dc.subjectProtein L23
dc.subject.lcshProteins--Crosslinking
dc.subject.lcshRibosomes
dc.titleThe signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosomeen_US
dc.typeArticleen_US
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