<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jiang Y</submitter><funding>NIGMS NIH HHS</funding><pagination>1149-61</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2290843</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>180(6)</volume><pubmed_abstract>The signal recognition particle (SRP)-dependent targeting pathway facilitates rapid, efficient delivery of the ribosome-nascent chain complex (RNC) to the protein translocation channel. We test whether the SRP receptor (SR) locates a vacant protein translocation channel by interacting with the yeast Sec61 and Ssh1 translocons. Surprisingly, the slow growth and cotranslational translocation defects caused by deletion of the transmembrane (TM) span of yeast SRbeta (SRbeta-DeltaTM) are exaggerated when the SSH1 gene is disrupted. Disruption of the SBH2 gene, which encodes the beta subunit of the Ssh1p complex, likewise causes a growth defect when combined with SRbeta-DeltaTM. Cotranslational translocation defects in the ssh1DeltaSRbeta-DeltaTM mutant are explained by slow and inefficient in v</pubmed_abstract><journal>The Journal of cell biology</journal><pubmed_title>An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.</pubmed_title><pmcid>PMC2290843</pmcid><funding_grant_id>GM35687</funding_grant_id><funding_grant_id>R01 GM035687</funding_grant_id><pubmed_authors>Jiang Y</pubmed_authors><pubmed_authors>Gilmore R</pubmed_authors><pubmed_authors>Mandon EC</pubmed_authors><pubmed_authors>Cheng Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.</name><description>The signal recognition particle (SRP)-dependent targeting pathway facilitates rapid, efficient delivery of the ribosome-nascent chain complex (RNC) to the protein translocation channel. We test whether the SRP receptor (SR) locates a vacant protein translocation channel by interacting with the yeast Sec61 and Ssh1 translocons. Surprisingly, the slow growth and cotranslational translocation defects caused by deletion of the transmembrane (TM) span of yeast SRbeta (SRbeta-DeltaTM) are exaggerated when the SSH1 gene is disrupted. Disruption of the SBH2 gene, which encodes the beta subunit of the Ssh1p complex, likewise causes a growth defect when combined with SRbeta-DeltaTM. Cotranslational translocation defects in the ssh1DeltaSRbeta-DeltaTM mutant are explained by slow and inefficient in v</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Mar</publication><modification>2025-04-22T07:05:51.486Z</modification><creation>2019-03-26T23:19:59Z</creation></dates><accession>S-EPMC2290843</accession><cross_references><pubmed>18347066</pubmed><doi>10.1083/jcb.200707196</doi></cross_references></HashMap>