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dc.contributor.authorRaden, David
dc.contributor.authorGilmore, Reid
dc.date2022-08-11T08:09:33.000
dc.date.accessioned2022-08-23T16:35:20Z
dc.date.available2022-08-23T16:35:20Z
dc.date.issued1998-03-14
dc.date.submitted2009-03-24
dc.identifier.citationMol Biol Cell. 1998 Jan;9(1):117-30.
dc.identifier.issn1059-1524 (Print)
dc.identifier.pmid9436995
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38535
dc.description.abstractProteins with RER-specific signal sequences are cotranslationally translocated across the rough endoplasmic reticulum through a proteinaceous channel composed of oligomers of the Sec61 complex. The Sec61 complex also binds ribosomes with high affinity. The dual function of the Sec61 complex necessitates a mechanism to prevent signal sequence-independent binding of ribosomes to the translocation channel. We have examined the hypothesis that the signal recognition particle (SRP) and the nascent polypeptide-associated complex (NAC), respectively, act as positive and negative regulatory factors to mediate the signal sequence-specific attachment of the ribosome-nascent chain complex (RNC) to the translocation channel. Here, SRP-independent translocation of a nascent secretory polypeptide was shown to occur in the presence of endogenous wheat germ or rabbit reticulocyte NAC. Furthermore, SRP markedly enhanced RNC binding to the translocation channel irrespective of the presence of NAC. Binding of RNCs, but not SRP-RNCs, to the Sec61 complex is competitively inhibited by 80S ribosomes. Thus, the SRP-dependent targeting pathway provides a mechanism for delivery of RNCs to the translocation channel that is not inhibited by the nonselective interaction between the ribosome and the Sec61 complex.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9436995&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAnimals
dc.subjectBinding, Competitive
dc.subjectBiological Transport
dc.subjectDogs
dc.subjectEndoplasmic Reticulum, Rough
dc.subjectMolecular Chaperones
dc.subjectPancreas
dc.subjectProtein Processing, Post-Translational
dc.subjectProtein Sorting Signals
dc.subjectProteins
dc.subjectRabbits
dc.subjectRibosomes
dc.subjectSeeds
dc.subjectSignal Recognition Particle
dc.subject*Trans-Activators
dc.subjectTriticum
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSignal recognition particle-dependent targeting of ribosomes to the rough endoplasmic reticulum in the absence and presence of the nascent polypeptide-associated complex
dc.typeArticle
dc.source.journaltitleMolecular biology of the cell
dc.source.volume9
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2404&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1405
dc.identifier.contextkey794902
refterms.dateFOA2022-08-23T16:35:20Z
html.description.abstract<p>Proteins with RER-specific signal sequences are cotranslationally translocated across the rough endoplasmic reticulum through a proteinaceous channel composed of oligomers of the Sec61 complex. The Sec61 complex also binds ribosomes with high affinity. The dual function of the Sec61 complex necessitates a mechanism to prevent signal sequence-independent binding of ribosomes to the translocation channel. We have examined the hypothesis that the signal recognition particle (SRP) and the nascent polypeptide-associated complex (NAC), respectively, act as positive and negative regulatory factors to mediate the signal sequence-specific attachment of the ribosome-nascent chain complex (RNC) to the translocation channel. Here, SRP-independent translocation of a nascent secretory polypeptide was shown to occur in the presence of endogenous wheat germ or rabbit reticulocyte NAC. Furthermore, SRP markedly enhanced RNC binding to the translocation channel irrespective of the presence of NAC. Binding of RNCs, but not SRP-RNCs, to the Sec61 complex is competitively inhibited by 80S ribosomes. Thus, the SRP-dependent targeting pathway provides a mechanism for delivery of RNCs to the translocation channel that is not inhibited by the nonselective interaction between the ribosome and the Sec61 complex.</p>
dc.identifier.submissionpathoapubs/1405
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.source.pages117-30


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