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dc.contributor.authorHofmann, A
dc.contributor.authorTarasov, S
dc.contributor.authorGrella, M
dc.contributor.authorRuvinov, S
dc.contributor.authorNasr, F
dc.contributor.authorFilipowicz, W
dc.contributor.authorWlodawer, A
dc.date.accessioned2017-05-03T15:19:26Z
dc.date.available2017-05-03T15:19:26Z
dc.date.issued2002
dc.date.modified2009-04-17T05:28:22Z
dc.identifier.issn0006-291X
dc.identifier.doi10.1006/bbrc.2002.6527
dc.identifier.urihttp://hdl.handle.net/10072/22212
dc.description.abstractWe have compared selected biophysical properties of three phosphodiesterases, from Arabidopsis thaliana, Saccharomyces cerevisiae, and Escherichia coli. All of them belong to a recently identified family of cyclic nucleotide phosphodiesterases. Experiments elucidating folding stability, protein fluorescence, oligomerization behavior, and the effects of substrates were conducted, revealing differences between the plant and the yeast protein. According to CD spectroscopy, the latter protein exhibits an (alpha + beta) fold rather than an (alpha/beta) fold as found with CPDase (A. thaliana). The redox-dependent structural reorganization recently found for the plant protein by X-ray crystallography could not be detected by CD spectroscopy due to its only marginal effect on the total percentage of helical content. However, in the present study a redox-dependent effect was also observed for the yeast CPDase. The enzymatic activity of wild type CPDase (A. thaliana) as well as of four mutants were characterized by isothermal titration calorimetry and the results prove the requirement of all four residues of the previously identified tandem signature motif for the catalytic function. Within the comparison of the three proteins in this study, the PDase Homolog/RNA ligase (E. coli) shares more similarities with the plant than with the yeast protein.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAcademic Press
dc.publisher.placeUnited States
dc.publisher.urihttp://www.sciencedirect.com/science/journal/0006291X
dc.relation.ispartofpagefrom875
dc.relation.ispartofpageto883
dc.relation.ispartofjournalBiochemical and biophysical research communications
dc.relation.ispartofvolume291
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchMedical biochemistry and metabolomics
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3205
dc.titleBiophysical Characterization of Cyclic Nucleotide Phosphodiesterases
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2002
gro.hasfulltextNo Full Text
gro.griffith.authorHofmann, Andreas


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