Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
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 evoluti...
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Main Authors: | Kevin E. W. Namitz, Tongyin Zheng, Ashley J. Canning, Nilda L. Alicea-Velazquez, Carlos A. Castañeda, Michael S. Cosgrove, Steven D. Hanes |
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Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2021
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Online Access: | https://doaj.org/article/cb36b1e1b4ac4118b1cc027bc944f7fe |
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