Communications Biology (Mar 2021)

Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism

  • Kevin E. W. Namitz,
  • Tongyin Zheng,
  • Ashley J. Canning,
  • Nilda L. Alicea-Velazquez,
  • Carlos A. Castañeda,
  • Michael S. Cosgrove,
  • Steven D. Hanes

DOI
https://doi.org/10.1038/s42003-021-01906-8
Journal volume & issue
Vol. 4, no. 1
pp. 1 – 14

Abstract

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Namitz, Zheng et al. identify a bivalent interaction by the yeast Ess1 with CTD peptides of RNA polymerase II. Their results suggest an anchored mechanism of isomerization, and raise the possibility of eukaryotic parvulin-class prolyl isomerases gaining a broader substrate specificity during evolution, by acquiring a flexible linker that generates a more dynamic binding mode.