Genetic interactions and transcriptomics implicate fission yeast CTD prolyl isomerase Pin1 as an agent of RNA 3' processing and transcription termination that functions via its effects on CTD phosphatase Ssu72 Journal Article

   

Authors:	Sanchez, A. M.; Garg, A.; Shuman, S.; Schwer, B.
Article Title:	Genetic interactions and transcriptomics implicate fission yeast CTD prolyl isomerase Pin1 as an agent of RNA 3' processing and transcription termination that functions via its effects on CTD phosphatase Ssu72
Abstract:	The phosphorylation pattern of Pol2 CTD Y1S2P3T4S5P6S7 repeats comprises an informational code coordinating transcription and RNA processing. cis-trans isomerization of CTD prolines expands the scope of the code in ways that are not well understood. Here we address this issue via analysis of fission yeast peptidyl-prolyl isomerase Pin1. A pin1Δ allele that does not affect growth per se is lethal in the absence of cleavage-polyadenylation factor (CPF) subunits Ppn1 and Swd22 and elicits growth defects absent CPF subunits Ctf1 and Dis2 and termination factor Rhn1. Whereas CTD S2A, T4A, and S7A mutants thrive in combination with pin1Δ, a Y1F mutant does not, nor do CTD mutants in which half the Pro3 or Pro6 residues are replaced by alanine. Phosphate-acquisition genes pho1, pho84 and tgp1 are repressed by upstream lncRNAs and are sensitive to changes in lncRNA 3' processing/termination. pin1Δ hyper-represses PHO gene expression and erases the de-repressive effect of CTD-S7A. Transcriptional profiling delineated sets of 56 and 22 protein-coding genes that are down-regulated and up-regulated in pin1Δ cells, respectively, 77% and 100% of which are downregulated/upregulated when the cis-proline-dependent Ssu72 CTD phosphatase is inactivated. Our results implicate Pin1 as a positive effector of 3' processing/termination that acts via Ssu72. © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
Journal Title:	Nucleic Acids Research
Volume:	48
Issue:	9
ISSN:	0305-1048
Publisher:	Oxford University Press
Date Published:	2020-05-21
Start Page:	4811
End Page:	4826
Language:	English
DOI:	10.1093/nar/gkaa212
PUBMED:	32282918
PROVIDER:	scopus
PMCID:	PMC7229847
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-85084935518&doi=10.1093%2fnar%2fgkaa212&partnerID=40&md5=002d30179d63349384cf3e329b1db54d
Notes:	Article -- Export Date: 1 June 2020 -- Source: Scopus

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