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Architecture of eukaryotic mRNA 3′-end processing machinery
by
Casañal, Ana
, Kumar, Ananthanarayanan
, Wiederhold, Katrin
, Degliesposti, Gianluca
, Wolf, Jana
, Gordiyenko, Yuliya
, Dornan, Gillian L.
, Passmore, Lori A.
, Skehel, Mark
, Easter, Ashley D.
, Hill, Chris H.
, Emsley, Paul
, Robinson, Carol V.
, Santhanam, Balaji
in
Cryoelectron Microscopy
/ Electron microscopy
/ Machinery and equipment
/ Mass spectrometry
/ Mass spectroscopy
/ Modules
/ mRNA Cleavage and Polyadenylation Factors - chemistry
/ mRNA Cleavage and Polyadenylation Factors - ultrastructure
/ Nuclease
/ Nucleic acids
/ Phosphatase
/ Polyadenylation
/ Polynucleotide Adenylyltransferase - metabolism
/ Propellers
/ Protein Conformation
/ Ribonucleic acid
/ RNA
/ RNA 3' End Processing
/ RNA Polymerase II - chemistry
/ RNA Polymerase II - ultrastructure
/ RNA, Messenger - metabolism
/ Saccharomyces cerevisiae - enzymology
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
/ Saccharomyces cerevisiae Proteins - ultrastructure
/ Substrates
/ Transcription termination
/ Yeast
2017
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Architecture of eukaryotic mRNA 3′-end processing machinery
by
Casañal, Ana
, Kumar, Ananthanarayanan
, Wiederhold, Katrin
, Degliesposti, Gianluca
, Wolf, Jana
, Gordiyenko, Yuliya
, Dornan, Gillian L.
, Passmore, Lori A.
, Skehel, Mark
, Easter, Ashley D.
, Hill, Chris H.
, Emsley, Paul
, Robinson, Carol V.
, Santhanam, Balaji
in
Cryoelectron Microscopy
/ Electron microscopy
/ Machinery and equipment
/ Mass spectrometry
/ Mass spectroscopy
/ Modules
/ mRNA Cleavage and Polyadenylation Factors - chemistry
/ mRNA Cleavage and Polyadenylation Factors - ultrastructure
/ Nuclease
/ Nucleic acids
/ Phosphatase
/ Polyadenylation
/ Polynucleotide Adenylyltransferase - metabolism
/ Propellers
/ Protein Conformation
/ Ribonucleic acid
/ RNA
/ RNA 3' End Processing
/ RNA Polymerase II - chemistry
/ RNA Polymerase II - ultrastructure
/ RNA, Messenger - metabolism
/ Saccharomyces cerevisiae - enzymology
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
/ Saccharomyces cerevisiae Proteins - ultrastructure
/ Substrates
/ Transcription termination
/ Yeast
2017
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Architecture of eukaryotic mRNA 3′-end processing machinery
by
Casañal, Ana
, Kumar, Ananthanarayanan
, Wiederhold, Katrin
, Degliesposti, Gianluca
, Wolf, Jana
, Gordiyenko, Yuliya
, Dornan, Gillian L.
, Passmore, Lori A.
, Skehel, Mark
, Easter, Ashley D.
, Hill, Chris H.
, Emsley, Paul
, Robinson, Carol V.
, Santhanam, Balaji
in
Cryoelectron Microscopy
/ Electron microscopy
/ Machinery and equipment
/ Mass spectrometry
/ Mass spectroscopy
/ Modules
/ mRNA Cleavage and Polyadenylation Factors - chemistry
/ mRNA Cleavage and Polyadenylation Factors - ultrastructure
/ Nuclease
/ Nucleic acids
/ Phosphatase
/ Polyadenylation
/ Polynucleotide Adenylyltransferase - metabolism
/ Propellers
/ Protein Conformation
/ Ribonucleic acid
/ RNA
/ RNA 3' End Processing
/ RNA Polymerase II - chemistry
/ RNA Polymerase II - ultrastructure
/ RNA, Messenger - metabolism
/ Saccharomyces cerevisiae - enzymology
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
/ Saccharomyces cerevisiae Proteins - ultrastructure
/ Substrates
/ Transcription termination
/ Yeast
2017
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Architecture of eukaryotic mRNA 3′-end processing machinery
Journal Article
Architecture of eukaryotic mRNA 3′-end processing machinery
2017
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Overview
Newly transcribed eukaryotic precursor messenger RNAs (pre-mRNAs) are processed at their 3′ ends by the ~1-megadalton multiprotein cleavage and polyadenylation factor (CPF). CPF cleaves pre-mRNAs, adds a polyadenylate tail, and triggers transcription termination, but it is unclear how its various enzymes are coordinated and assembled. Here, we show that the nuclease, polymerase, and phosphatase activities of yeast CPF are organized into three modules. Using electron cryomicroscopy, we determined a 3.5-angstrom-resolution structure of the ~200-kilodalton polymerase module. This revealed four β propellers, in an assembly markedly similar to those of other protein complexes that bind nucleic acid. Combined with in vitro reconstitution experiments, our data show that the polymerase module brings together factors required for specific and efficient polyadenylation, to help coordinate mRNA 3′-end processing.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Modules
/ mRNA Cleavage and Polyadenylation Factors - chemistry
/ mRNA Cleavage and Polyadenylation Factors - ultrastructure
/ Nuclease
/ Polynucleotide Adenylyltransferase - metabolism
/ RNA
/ RNA Polymerase II - chemistry
/ RNA Polymerase II - ultrastructure
/ Saccharomyces cerevisiae - enzymology
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
/ Saccharomyces cerevisiae Proteins - ultrastructure
/ Yeast
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