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dc.contributor.authorZalucki, Yaramahen_US
dc.contributor.authorE. Jones, Christopheren_US
dc.contributor.authorNg, Prestonen_US
dc.contributor.authorL. Schulz, Benjaminen_US
dc.contributor.authorJennings, Michaelen_US
dc.date.accessioned2017-05-03T15:42:34Z
dc.date.available2017-05-03T15:42:34Z
dc.date.issued2010en_US
dc.date.modified2010-10-06T06:56:19Z
dc.identifier.issn00052736en_US
dc.identifier.doi10.1016/j.bbamem.2010.03.010en_AU
dc.identifier.urihttp://hdl.handle.net/10072/34412
dc.description.abstractNon-optimal codons are generally characterised by a low concentration of isoaccepting tRNA and a slower translation rate compared to optimal codons. In a previous study, we reported a 20-fold reduction in maltose binding protein (MBP) level when the non-optimal codons in the signal sequence were optimised. In this study, we report that the 20-fold reduction is rescued when MBP is expressed at 28 degrees C instead of 37 degrees C, suggesting that the signal sequence optimised MBP protein (MBP-opt) may be misfolded, and is being degraded at 37 degrees C. Consistent with this idea, transient induction of the heat shock proteases prior to MBP expression at 28 degrees C restores the 20-fold difference, demonstrating that the difference in production levels is due to post-translational degradation of MBP-opt by the heat-shock proteases. Analysis of the structure of purified MBP-wt and MBP-opt grown at 28 degrees C showed that although they have similar secondary structure content, MBP-opt is more resistant to thermal unfolding than is MBP-wt. The two proteins also exhibit different tryptic fragment profiles, further confirming that they are folded into conformationally different states. This is the first study to demonstrate that signal sequence non-optimal codons can influence the folding of the mature exported protein.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeNetherlandsen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom1244en_US
dc.relation.ispartofpageto1249en_US
dc.relation.ispartofissue6en_US
dc.relation.ispartofjournalBiochimica et Biophysica Acta (BBA) - Biomembranesen_US
dc.relation.ispartofvolume1798en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchProtein Traffickingen_US
dc.subject.fieldofresearchcode060108en_US
dc.titleSignal sequence non-optimal codons are required for the correct folding of mature maltose binding proteinen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.date.issued2010
gro.hasfulltextNo Full Text


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