Abstract
Yeast Fpr4p belongs to the FK506-binding protein (FKBP) class of peptidyl proline isomerases (PPIases), and has been implicated in regulating the cis–trans conversion of proline residues within histone tails. Here we report the 1H, 13C and 15N chemical shift assignments for the bacterially expressed C-terminal PPIase catalytic domain of Fpr4p. Prediction of secondary structure reveals similarity to domains from other members of the FKBP proline isomerases, including yeast Fpr1p and the prototypic PPIase region from human FKBP12.
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Acknowledgments
We thank N. Sparks for assistance with cloning. This research was supported by funds from the Institut de Chimie des Substances Naturelles, the Aquitaine regional government, the Institut Européen de Chimie et Biologie, the French national equipment network for NMR spectroscopy (TGE RMN THC Fr3050) and the National Sciences and Engineering Research Council (NSERC 371680).
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Monneau, Y.R., Nelson, C.J. & Mackereth, C.D. Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p. Biomol NMR Assign 6, 123–126 (2012). https://doi.org/10.1007/s12104-011-9338-x
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DOI: https://doi.org/10.1007/s12104-011-9338-x