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.
Cell Cycle Proteins
/ chemistry
Cleavage And Polyadenylation Specificity Factor
/ genetics
Gene Deletion
Gene Expression Regulation, Fungal
NIMA-Interacting Peptidylprolyl Isomerase
/ chemistry
Nuclear Proteins
/ genetics
Peptidylprolyl Isomerase
/ chemistry
Phosphates
/ metabolism
Phosphoprotein Phosphatases
/ genetics
Phosphorylation
Protein Domains
/ genetics
Pyrophosphatases
/ genetics
RNA 3' End Processing
RNA Polymerase II
/ genetics
RNA-Seq
Regulon
Schizosaccharomyces
/ enzymology
Schizosaccharomyces pombe Proteins
/ chemistry
Serine
/ metabolism
Threonine
/ metabolism
Transcription Termination, Genetic
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
21 05 2020
21 05 2020
Historique:
accepted:
24
03
2020
revised:
19
03
2020
received:
24
01
2020
pubmed:
14
4
2020
medline:
9
9
2020
entrez:
14
4
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32282918
pii: 5819598
doi: 10.1093/nar/gkaa212
pmc: PMC7229847
doi:
Substances chimiques
Cell Cycle Proteins
0
Cleavage And Polyadenylation Specificity Factor
0
NIMA-Interacting Peptidylprolyl Isomerase
0
Nuclear Proteins
0
Phosphates
0
Rhn1 protein, S pombe
0
Schizosaccharomyces pombe Proteins
0
Threonine
2ZD004190S
Serine
452VLY9402
RNA Polymerase II
EC 2.7.7.-
Rpb1 protein, S pombe
EC 2.7.7.-
Phosphoprotein Phosphatases
EC 3.1.3.16
ssu72 protein, S pombe
EC 3.1.3.16
Pyrophosphatases
EC 3.6.1.-
aps1 protein, S pombe
EC 3.6.1.-
Peptidylprolyl Isomerase
EC 5.2.1.8
pin1 protein, S pombe
EC 5.2.1.8
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
4811-4826Subventions
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM052470
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM134021
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM126945
Pays : United States
Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
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