Document Detail


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.
MedLine Citation:
PMID:  19188448     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Mohamed A Ghazy; Xiaoyuan He; Badri Nath Singh; Michael Hampsey; Claire Moore
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2009-02-02
Journal Detail:
Title:  Molecular and cellular biology     Volume:  29     ISSN:  1098-5549     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2009 Apr 
Date Detail:
Created Date:  2009-03-27     Completed Date:  2009-04-22     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2296-307     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.
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MeSH Terms
Descriptor/Qualifier:
Carrier Proteins / physiology*
Mutant Proteins
Phosphoprotein Phosphatases
Polyadenylation
RNA 3' End Processing*
RNA Precursors / metabolism*
RNA, Small Nucleolar / genetics*
Saccharomyces cerevisiae Proteins / chemistry,  physiology*
Sequence Deletion
Transcription, Genetic*
mRNA Cleavage and Polyadenylation Factors / chemistry,  physiology*
Grant Support
ID/Acronym/Agency:
GM39484/GM/NIGMS NIH HHS; GM41752/GM/NIGMS NIH HHS; GM68887/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Mutant Proteins; 0/PTA1 protein, S cerevisiae; 0/RNA Precursors; 0/RNA, Small Nucleolar; 0/SSU72 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/mRNA Cleavage and Polyadenylation Factors; EC 3.1.3.16/Phosphoprotein Phosphatases
Comments/Corrections

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