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Extensive lysine methylation in hyperthermophilic crenarchaea : potential implications for protein stability and recombinant enzymes
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dc.contributor.author | Botting, Catherine H. | |
dc.contributor.author | Talbot, Paul | |
dc.contributor.author | Paytubi, Sonia | |
dc.contributor.author | White, Malcolm F. | |
dc.date.accessioned | 2014-05-07T11:01:02Z | |
dc.date.available | 2014-05-07T11:01:02Z | |
dc.date.issued | 2010 | |
dc.identifier.citation | Botting , C H , Talbot , P , Paytubi , S & White , M F 2010 , ' Extensive lysine methylation in hyperthermophilic crenarchaea : potential implications for protein stability and recombinant enzymes ' , Archaea , vol. 2010 , 106341 . https://doi.org/10.1155/2010/106341 | en |
dc.identifier.issn | 1472-3646 | |
dc.identifier.other | PURE: 7308534 | |
dc.identifier.other | PURE UUID: bdbb0347-c86d-4750-ba76-43f7feabde8b | |
dc.identifier.other | WOS: 000288787700001 | |
dc.identifier.other | Scopus: 77956809497 | |
dc.identifier.other | ORCID: /0000-0003-1543-9342/work/47136071 | |
dc.identifier.uri | https://hdl.handle.net/10023/4718 | |
dc.description.abstract | In eukarya and bacteria, lysine methylation is relatively rare and is catalysed by sequence-specific lysine methyltransferases that typically have only a single-protein target. Using RNA polymerase purified from the thermophilic crenarchaeum Sulfolobus solfataricus, we identified 21 methyllysines distributed across 9 subunits of the enzyme. The modified lysines were predominantly in alpha-helices and showed no conserved sequence context. A limited survey of the Thermoproteus tenax proteome revealed widespread modification with 52 methyllysines in 30 different proteins. These observations suggest the presence of an unusual lysine methyltransferase with relaxed specificity in the crenarchaea. Since lysine methylation is known to enhance protein thermostability, this may be an adaptation to a thermophilic lifestyle. The implications of this modification for studies and applications of recombinant crenarchaeal enzymes are discussed. | |
dc.format.extent | 6 | |
dc.language.iso | eng | |
dc.relation.ispartof | Archaea | en |
dc.rights | Copyright © 2010 Botting et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. | en |
dc.subject | Sulfolobus-solfataricus | en |
dc.subject | Posttranslational modifications | en |
dc.subject | Glutamate-dehydrogenase | en |
dc.subject | Pyrococcus-furiosus | en |
dc.subject | Proteomics | en |
dc.subject | Sequence | en |
dc.subject | Archaebacterium | en |
dc.subject | Acetylation | en |
dc.subject | Rubisco | en |
dc.subject | RNA | en |
dc.subject | QH301 Biology | en |
dc.subject.lcc | QH301 | en |
dc.title | Extensive lysine methylation in hyperthermophilic crenarchaea : potential implications for protein stability and recombinant enzymes | en |
dc.type | Journal article | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.identifier.doi | https://doi.org/10.1155/2010/106341 | |
dc.description.status | Peer reviewed | en |
dc.identifier.url | http://ukpmc.ac.uk/abstract/MED/20811616 | en |
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