ArticleMolecular and cellular biology2009
The essential N terminus of the Pta1 scaffold protein is required for snoRNA transcription termination and Ssu72 function but is dispensable for pre-mRNA 3'-end processing.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 60 citations in OpenAlex.
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- Review
- ThrScience advances · 2024Article
- Article
- Birth of a poly(A) tail: mechanisms and control of mRNA polyadenylation.FEBS open bio · 2023Review
- Natural variation in the plant polyadenylation complex.Frontiers in plant science · 2023Article
- Fip1 is a multivalent interaction scaffold for processing factors in human mRNA 3' end biogenesis.eLife · 2022Article
- Mammalian Ssu72 phosphatase preferentially considers tissue-specific actively transcribed gene expression by regulating RNA Pol II transcription.Theranostics · 2022Article
- U7 deciphered: the mechanism that forms the unusual 3' end of metazoan replication-dependent histone mRNAs.Biochemical Society transactions · 2021Review
- Dynamics in Fip1 regulate eukaryotic mRNA 3' end processing.Genes & development · 2021Article
- Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.Cell reports · 2021Article
- Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases.International journal of molecular sciences · 2021Review
- Diverse and conserved roles of the protein Ssu72 in eukaryotes: from yeast to higher organisms.Current genetics · 2021Review
- Regulation of the Ysh1 endonuclease of the mRNA cleavage/polyadenylation complex by ubiquitin-mediated degradation.RNA biology · 2020Article
- Recent molecular insights into canonical pre-mRNA 3'-end processing.Transcription · 2020Review
- Dense Transposon Integration Reveals Essential Cleavage and Polyadenylation Factors Promote Heterochromatin Formation.Cell reports · 2020Article
- Structural Insights into the Human Pre-mRNA 3'-End Processing Machinery.Molecular cell · 2020Article
- Structure of an active human histone pre-mRNA 3'-end processing machinery.Science (New York, N.Y.) · 2020Article
- Structural determinants for accurate dephosphorylation of RNA polymerase II by its cognate C-terminal domain (CTD) phosphatase during eukaryotic transcription.The Journal of biological chemistry · 2019Article
- The APT complex is involved in non-coding RNA transcription and is distinct from CPF.Nucleic acids research · 2018Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
Saccharomyces cerevisiae Pta1 is a component of the cleavage/polyadenylation factor (CPF) 3'-end processing complex and functions in pre-mRNA cleavage, poly(A) addition, and transcription termination. In this study, we investigated the role of the N-terminal region of Pta1 in transcription and processing. We report that a deletion of the first 75 amino acids (pta1-Delta75) causes thermosensitive growth, while the deletion of an additional 25 amino acids is lethal. The pta1-Delta75 mutant is defective for snoRNA termination, RNA polymerase II C-terminal domain Ser5-P dephosphorylation, and gene looping but is fully functional for mRNA 3'-end processing. Furthermore, different regions of Pta1 interact with the CPF subunits Ssu72, Pti1, and Ysh1, supporting the idea that Pta1 acts as a scaffold to organize CPF. The first 300 amino acids of Pta1 are sufficient for interactions with Ssu72, which is needed for pre-mRNA cleavage. By the degron-mediated depletion of Pta1, we show that the removal of this essential region leads to a loss of Ssu72, yet surprisingly, in vitro cleavage and polyadenylation remain efficient. In addition, a fragment containing amino acids 1 to 300 suppresses 3'-end processing in wild-type extracts. These findings suggest that the amino terminus of Pta1 has an inhibitory effect and that this effect can be neutralized through the interaction with Ssu72.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.