Structural highlights
Publication Abstract from PubMed
Accurate gene transcription in eukaryotes depends on isomerization of serine-proline bonds within the carboxy-terminal domain (CTD) of RNA polymerase II. Isomerization is part of the "CTD code" that regulates recruitment of proteins required for transcription and co-transcriptional RNA processing. Saccharomyces cerevisiae Ess1 and its human ortholog, Pin1, are prolyl isomerases that engage the long heptad repeat (YSPTSPS)26 of the CTD by an unknown mechanism. Here, we used an integrative structural approach to decipher Ess1 interactions with the CTD. Ess1 has a rigid linker between its WW and catalytic domains that enforces a distance constraint for bivalent interaction with the ends of long CTD substrates (>/=4-5 heptad repeats). Our binding results suggest that the Ess1 WW domain anchors the proximal end of the CTD substrate during isomerization, and that linker divergence may underlie evolution of substrate specificity.
Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.,Namitz KEW, Zheng T, Canning AJ, Alicea-Velazquez NL, Castaneda CA, Cosgrove MS, Hanes SD Commun Biol. 2021 Mar 25;4(1):398. doi: 10.1038/s42003-021-01906-8. PMID:33767358[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Namitz KEW, Zheng T, Canning AJ, Alicea-Velazquez NL, Castaneda CA, Cosgrove MS, Hanes SD. Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism. Commun Biol. 2021 Mar 25;4(1):398. doi: 10.1038/s42003-021-01906-8. PMID:33767358 doi:http://dx.doi.org/10.1038/s42003-021-01906-8
