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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Autores principales:	Kevin E. W. Namitz, Tongyin Zheng, Ashley J. Canning, Nilda L. Alicea-Velazquez, Carlos A. Castañeda, Michael S. Cosgrove, Steven D. Hanes
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/cb36b1e1b4ac4118b1cc027bc944f7fe
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spelling	oai:doaj.org-article:cb36b1e1b4ac4118b1cc027bc944f7fe2021-12-02T17:04:04ZStructure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism10.1038/s42003-021-01906-82399-3642https://doaj.org/article/cb36b1e1b4ac4118b1cc027bc944f7fe2021-03-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01906-8https://doaj.org/toc/2399-3642Namitz, 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.Kevin E. W. NamitzTongyin ZhengAshley J. CanningNilda L. Alicea-VelazquezCarlos A. CastañedaMichael S. CosgroveSteven D. HanesNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Kevin E. W. Namitz Tongyin Zheng Ashley J. Canning Nilda L. Alicea-Velazquez Carlos A. Castañeda Michael S. Cosgrove Steven D. Hanes Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
description	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.
format	article
author	Kevin E. W. Namitz Tongyin Zheng Ashley J. Canning Nilda L. Alicea-Velazquez Carlos A. Castañeda Michael S. Cosgrove Steven D. Hanes
author_facet	Kevin E. W. Namitz Tongyin Zheng Ashley J. Canning Nilda L. Alicea-Velazquez Carlos A. Castañeda Michael S. Cosgrove Steven D. Hanes
author_sort	Kevin E. W. Namitz
title	Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
title_short	Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
title_full	Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
title_fullStr	Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
title_full_unstemmed	Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism
title_sort	structure analysis suggests ess1 isomerizes the carboxy-terminal domain of rna polymerase ii via a bivalent anchoring mechanism
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/cb36b1e1b4ac4118b1cc027bc944f7fe
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Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism

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