Mittelstät, Jörg

[["dc.bibliographiccitation.firstpage","341"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","351"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Buhr, Florian"],["dc.contributor.author","Jha, Sujata"],["dc.contributor.author","Thommen, Michael"],["dc.contributor.author","Mittelstaet, Joerg"],["dc.contributor.author","Kutz, Felicitas"],["dc.contributor.author","Schwalbe, Harald"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Komar, Anton A."],["dc.date.accessioned","2017-09-07T11:54:38Z"],["dc.date.available","2017-09-07T11:54:38Z"],["dc.date.issued","2016"],["dc.description.abstract","In all genomes, most amino acids are encoded by more than one codon. Synonymous codons can modulate protein production and folding, but the mechanism connecting codon usage to protein homeostasis is not known. Here we show that synonymous codon variants in the gene encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotranslational folding of protein domains monitored in real time by Forster resonance energy transfer and fluorescence-intensity changes. Gamma-B crystallins produced from mRNAs with changed codon bias have the same amino acid sequence but attain different conformations, as indicated by altered in vivo stability and in vitro protease resistance. 2D NMR spectroscopic data suggest that structural differences are associated with different cysteine oxidation states of the purified proteins, providing a link between translation, folding, and the structures of isolated proteins. Thus, synonymous codons provide a secondary code for protein folding in the cell."],["dc.identifier.doi","10.1016/j.molcel.2016.01.008"],["dc.identifier.gro","3141730"],["dc.identifier.isi","000372325800004"],["dc.identifier.pmid","26849192"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/435"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1097-4164"],["dc.relation.issn","1097-2765"],["dc.title","Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1104"],["dc.bibliographiccitation.issue","6264"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1107"],["dc.bibliographiccitation.volume","350"],["dc.contributor.author","Holtkamp, Wolf"],["dc.contributor.author","Kokic, Goran"],["dc.contributor.author","Jäger, Marcus"],["dc.contributor.author","Mittelstaet, Joerg"],["dc.contributor.author","Komar, Anton A."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:54:52Z"],["dc.date.available","2017-09-07T11:54:52Z"],["dc.date.issued","2015"],["dc.description.abstract","Protein domains can fold into stable tertiary structures while they are synthesized on the ribosome. We used a high-performance, reconstituted in vitro translation system to investigate the folding of a small five-helix protein domain-the N-terminal domain of Escherichia coli N5-glutamine methyltransferase HemK-in real time. Our observations show that cotranslational folding of the protein, which folds autonomously and rapidly in solution, proceeds through a compact, non-native conformation that forms within the peptide tunnel of the ribosome. The compact state rearranges into a native-like structure immediately after the full domain sequence has emerged from the ribosome. Both folding transitions are rate-limited by translation, allowing for quasi-equilibrium sampling of the conformational space restricted by the ribosome. Cotranslational folding may be typical of small, intrinsically rapidly folding protein domains."],["dc.identifier.doi","10.1126/science.aad0344"],["dc.identifier.gro","3141785"],["dc.identifier.isi","000366422600047"],["dc.identifier.pmid","26612953"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1046"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Cotranslational protein folding on the ribosome monitored in real time"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]