Bornemann, Thomas

[["dc.bibliographiccitation.artnumber","5263"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.lastpage","6"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Ge, Yan"],["dc.contributor.author","Draycheva, Albena"],["dc.contributor.author","Bornemann, Thomas"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:45:28Z"],["dc.date.available","2017-09-07T11:45:28Z"],["dc.date.issued","2014"],["dc.description.abstract","Proteins are co-translationally inserted into the bacterial plasma membrane via the SecYEG translocon by lateral release of hydrophobic transmembrane segments into the phospholipid bilayer. The trigger for lateral opening of the translocon is not known. Here we monitor lateral opening by photo-induced electron transfer (PET) between two fluorophores attached to the two SecY helices at the rim of the gate. In the resting translocon, the fluorescence is quenched, consistent with a closed conformation. Ribosome binding to the translocon diminishes PET quenching, indicating opening of the gate. The effect is larger with ribosomes exposing hydrophobic transmembrane segments and vanishes at low temperature. We propose a temperature-dependent dynamic equilibrium between closed and open conformations of the translocon that is shifted towards partially and fully open by ribosome binding and insertion of a hydrophobic peptide, respectively. The combined effects of ribosome and peptide binding allow for co-translational membrane insertion of successive transmembrane segments."],["dc.identifier.doi","10.1038/ncomms6263"],["dc.identifier.gro","3142041"],["dc.identifier.isi","000343985700002"],["dc.identifier.pmid","25314960"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3889"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2041-1723"],["dc.title","Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","494"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","499"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Bornemann, Thomas"],["dc.contributor.author","Jöckel, Johannes"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:48:44Z"],["dc.date.available","2017-09-07T11:48:44Z"],["dc.date.issued","2008"],["dc.description.abstract","Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the translocon in the plasma membrane by the signal recognition particle (SRP) and the SRP receptor, FtsY. Here we show using a purified system that membrane targeting does not require an exposed signal-anchor sequence, as SRP-dependent targeting takes place with ribosomes containing short nascent peptides, with or without a signal-anchor sequence, within the peptide exit tunnel. Signaling from inside the tunnel involves ribosomal protein L23, which constitutes part of the SRP binding site. When nascent peptides emerge from the ribosome, the targeting complex is maintained with ribosomes exposing a signal-anchor sequence, whereas ribosomes exposing other sequences are released. These results indicate that ribosome-nascent chain complexes containing any nascent peptide within the exit tunnel can enter the SRP targeting pathway to be sorted at the membrane into ribosome-nascent chain complexes that synthesize either membrane or cytosolic proteins."],["dc.identifier.doi","10.1038/nsmb.1402"],["dc.identifier.gro","3143312"],["dc.identifier.isi","000255587800017"],["dc.identifier.pmid","18391966"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/812"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9985"],["dc.title","Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","207"],["dc.bibliographiccitation.journal","Journal of Building Engineering"],["dc.bibliographiccitation.lastpage","215"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Brischke, C."],["dc.contributor.author","Meyer-Veltrup, L."],["dc.contributor.author","Bornemann, T."],["dc.date.accessioned","2020-12-10T14:25:15Z"],["dc.date.available","2020-12-10T14:25:15Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.jobe.2017.08.004"],["dc.identifier.issn","2352-7102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72501"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Moisture performance and durability of wooden façades and decking during six years of outdoor exposure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1332"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Nature structural & molecular biology"],["dc.bibliographiccitation.lastpage","1337"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Holtkamp, Wolf"],["dc.contributor.author","Lee, Sejeong"],["dc.contributor.author","Bornemann, Thomas"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2018-01-29T11:01:49Z"],["dc.date.available","2018-01-29T11:01:49Z"],["dc.date.issued","2012"],["dc.description.abstract","Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the membrane by the signal recognition particle (SRP) pathway. By rapid kinetic analysis we show that after initial binding to the ribosome, SRP undergoes dynamic fluctuations in search of additional interactions. Non-translating ribosomes, or ribosomes synthesizing non-membrane proteins, do not provide these contacts, allowing SRPs to dissociate rapidly. A nascent peptide in the exit tunnel stabilizes SRPs in a standby state. Binding to the emerging signal-anchor sequence (SAS) of a nascent membrane protein halts the fluctuations of SRP, resulting in complex stabilization and recruitment of the SRP receptor. We propose a kinetic model where SRP rapidly scans all ribosomes until it encounters a ribosome exposing an SAS. Binding to the SAS switches SRP into the targeting mode, in which dissociation is slow and docking of the SRP receptor is accelerated."],["dc.identifier.doi","10.1038/nsmb.2421"],["dc.identifier.pmid","23142984"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11868"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1545-9985"],["dc.title","Dynamic switch of the signal recognition particle from scanning to targeting"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","402a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Rodnin, Dmytro"],["dc.contributor.author","Sanabria, Hugo"],["dc.contributor.author","Fekekyan, Suren"],["dc.contributor.author","Kalinin, Stanislav"],["dc.contributor.author","Bornemann, Thomas"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Seidel, Claus"],["dc.date.accessioned","2022-03-01T11:44:55Z"],["dc.date.available","2022-03-01T11:44:55Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1016/j.bpj.2011.11.2193"],["dc.identifier.pii","S0006349511035417"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103159"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Homo-FRET Studies of the Signal Recognition Particle Protein FFH by Multiparameter Fluorescence Detection (MFD) and Filtered Fluorescence Correlation Spectroscopy (FFCs)"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]