Nuclear mRNA Surveillance in THO/sub2 Mutants Is Triggered by Inefficient Polyadenylation
The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of t...
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| Published in | Molecular cell Vol. 31; no. 1; pp. 91 - 103 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
11.07.2008
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| Abstract | The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of this accelerated mRNA decay. A genetic screen reveals extensive interactions between deletions of THO subunits and mRNA 3′ end processing mutants. Nuclear run-ons strengthen this link by showing premature transcription termination close to polyadenylation sites in THO/sub2 mutants in vivo. Moreover, in vitro, pre-mRNA substrates are poorly polyadenylated and consequently unstable in extracts from THO/sub2 mutant strains. Decreased polyadenylation correlates with a specific downregulation of the poly(A)-polymerase cofactor Fip1p by the ubiquitin/proteasome pathway. Both polyadenylation defects and Fip1p instability depend on the nuclear exosome component Rrp6p and its activator Trf4p. We suggest that removal of aberrant mRNA is facilitated by direct regulation of polyadenylation activity. |
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| AbstractList | The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of this accelerated mRNA decay. A genetic screen reveals extensive interactions between deletions of THO subunits and mRNA 3' end processing mutants. Nuclear run-ons strengthen this link by showing premature transcription termination close to polyadenylation sites in THO/sub2 mutants in vivo. Moreover, in vitro, pre-mRNA substrates are poorly polyadenylated and consequently unstable in extracts from THO/sub2 mutant strains. Decreased polyadenylation correlates with a specific downregulation of the poly(A)-polymerase cofactor Fip1p by the ubiquitin/proteasome pathway. Both polyadenylation defects and Fip1p instability depend on the nuclear exosome component Rrp6p and its activator Trf4p. We suggest that removal of aberrant mRNA is facilitated by direct regulation of polyadenylation activity.The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of this accelerated mRNA decay. A genetic screen reveals extensive interactions between deletions of THO subunits and mRNA 3' end processing mutants. Nuclear run-ons strengthen this link by showing premature transcription termination close to polyadenylation sites in THO/sub2 mutants in vivo. Moreover, in vitro, pre-mRNA substrates are poorly polyadenylated and consequently unstable in extracts from THO/sub2 mutant strains. Decreased polyadenylation correlates with a specific downregulation of the poly(A)-polymerase cofactor Fip1p by the ubiquitin/proteasome pathway. Both polyadenylation defects and Fip1p instability depend on the nuclear exosome component Rrp6p and its activator Trf4p. We suggest that removal of aberrant mRNA is facilitated by direct regulation of polyadenylation activity. The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of this accelerated mRNA decay. A genetic screen reveals extensive interactions between deletions of THO subunits and mRNA 3′ end processing mutants. Nuclear run-ons strengthen this link by showing premature transcription termination close to polyadenylation sites in THO/sub2 mutants in vivo. Moreover, in vitro, pre-mRNA substrates are poorly polyadenylated and consequently unstable in extracts from THO/sub2 mutant strains. Decreased polyadenylation correlates with a specific downregulation of the poly(A)-polymerase cofactor Fip1p by the ubiquitin/proteasome pathway. Both polyadenylation defects and Fip1p instability depend on the nuclear exosome component Rrp6p and its activator Trf4p. We suggest that removal of aberrant mRNA is facilitated by direct regulation of polyadenylation activity. The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to degradation by a surveillance mechanism that involves the nuclear RNA exosome. Here we show that inefficient polyadenylation forms the basis of this accelerated mRNA decay. A genetic screen reveals extensive interactions between deletions of THO subunits and mRNA 3' end processing mutants. Nuclear run-ons strengthen this link by showing premature transcription termination close to polyadenylation sites in THO/sub2 mutants in vivo. Moreover, in vitro, pre-mRNA substrates are poorly polyadenylated and consequently unstable in extracts from THO/sub2 mutant strains. Decreased polyadenylation correlates with a specific downregulation of the poly(A)-polymerase cofactor Fip1p by the ubiquitin/proteasome pathway. Both polyadenylation defects and Fip1p instability depend on the nuclear exosome component Rrp6p and its activator Trf4p. We suggest that removal of aberrant mRNA is facilitated by direct regulation of polyadenylation activity. |
| Author | Schmid, Manfred Ghazy, Mohamed Abd El-Hady Olesen, Jens Raabjerg Moore, Claire Qu, Xiangping Nasser, Tommy Jensen, Torben Heick Poulsen, Mathias Bach Saguez, Cyril |
| Author_xml | – sequence: 1 givenname: Cyril surname: Saguez fullname: Saguez, Cyril organization: Centre for mRNP Biogenesis and Metabolism, Aarhus University, C.F. Møllers Alle, Building 130, DK-8000 Aarhus C, Denmark – sequence: 2 givenname: Manfred surname: Schmid fullname: Schmid, Manfred organization: Centre for mRNP Biogenesis and Metabolism, Aarhus University, C.F. Møllers Alle, Building 130, DK-8000 Aarhus C, Denmark – sequence: 3 givenname: Jens Raabjerg surname: Olesen fullname: Olesen, Jens Raabjerg organization: Centre for mRNP Biogenesis and Metabolism, Aarhus University, C.F. Møllers Alle, Building 130, DK-8000 Aarhus C, Denmark – sequence: 4 givenname: Mohamed Abd El-Hady surname: Ghazy fullname: Ghazy, Mohamed Abd El-Hady organization: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA – sequence: 5 givenname: Xiangping surname: Qu fullname: Qu, Xiangping organization: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA – sequence: 6 givenname: Mathias Bach surname: Poulsen fullname: Poulsen, Mathias Bach organization: Centre for mRNP Biogenesis and Metabolism, Aarhus University, C.F. Møllers Alle, Building 130, DK-8000 Aarhus C, Denmark – sequence: 7 givenname: Tommy surname: Nasser fullname: Nasser, Tommy organization: Centre for mRNP Biogenesis and Metabolism, Aarhus University, C.F. Møllers Alle, Building 130, DK-8000 Aarhus C, Denmark – sequence: 8 givenname: Claire surname: Moore fullname: Moore, Claire organization: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA – sequence: 9 givenname: Torben Heick surname: Jensen fullname: Jensen, Torben Heick email: thj@mb.au.dk organization: Centre for mRNP Biogenesis and Metabolism, Aarhus University, C.F. Møllers Alle, Building 130, DK-8000 Aarhus C, Denmark |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18614048$$D View this record in MEDLINE/PubMed |
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| Snippet | The yeast THO complex and the associated RNA helicase Sub2p are important mRNP maturation factors. Transcripts produced in THO/sub2 mutants are subject to... |
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| SubjectTerms | Adenosine Triphosphatases - metabolism Amino Acid Transport Systems - metabolism Cell Nucleus - metabolism Codon, Nonsense Down-Regulation mRNA Cleavage and Polyadenylation Factors - metabolism Multiprotein Complexes - metabolism Mutation - genetics Poly A - metabolism Polyadenylation Proteasome Endopeptidase Complex - metabolism RNA RNA Precursors - metabolism RNA Stability RNA, Fungal - metabolism RNA, Messenger Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - metabolism Transcription, Genetic Ubiquitin - metabolism |
| Title | Nuclear mRNA Surveillance in THO/sub2 Mutants Is Triggered by Inefficient Polyadenylation |
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