Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3′-end formation
Copyright policy )Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3′-end formation
Hrp1p is a heterogeneous ribonucleoprotein (hnRNP) from the yeast Saccharomyces cerevisiae that is involved in the cleavage and polyadenylation of the 3'-end of mRNAs and mRNA export. In addition, Hrplp is one of several RNA-binding proteins that are posttranslationally modified by methylation at arginine residues. By using functional recombinant Hrp1p, we have identified RNA sequences with specific high affinity binding sites. These sites correspond to the efficiency element for mRNA 3'-end formation, UAUAUA. To examine the effect of methylation on specific RNA binding, purified recombinant arginine methyltransferase (Hmt1p) was used to methylate Hrp1p. Methylated Hrp1p binds with the same affinity to UAUAUA-containing RNAs as unmethylated Hrpl p indicating that methylation does not affect specific RNA binding. However, RNA itself inhibits the methylation of Hrp1p and this inhibition is enhanced by RNAs that specifically bind Hrpl p. Taken together, these data support a model in which protein methylation occurs prior to protein-RNA binding in the nucleus.
- Harvard University United States
- Sao Paulo State University Brazil
- Dana-Farber Cancer Institute United States
- Universidade Estadual Paulista - UNESP Brazil
Protein-Arginine N-Methyltransferases, Messenger, arginine, Heterogeneous-Nuclear Ribonucleoproteins, saccharomyces cerevisiae, Adenosine Triphosphatases, messenger RNA, Intracellular Signaling Peptides and Proteins, RNA-Binding Proteins, hnRNPs, Recombinant Proteins, unclassified drug, Cross-Linking Reagents, priority journal, Ribonucleoproteins, ribonucleoprotein hrp1p, protein RNA binding, Hmt1p, Protein Binding, Molecular Sequence Data, RNA sequence, Polyadenylation, Arginine, Methylation, ribonucleoprotein, reverse transcription polymerase chain reaction, controlled study, Amino Acid Sequence, RNA, Messenger, protein methylation, Protein Processing, Cleavage, nonhuman, Binding Sites, Oligoribonucleotides, Base Sequence, binding site, cell nucleus, Post-Translational, DNA Helicases, RNA cleavage, Methyltransferases, RNA binding, RNA binding protein, Kinetics, RNA processing, RNA, methyltransferase, Protein Processing, Post-Translational
Protein-Arginine N-Methyltransferases, Messenger, arginine, Heterogeneous-Nuclear Ribonucleoproteins, saccharomyces cerevisiae, Adenosine Triphosphatases, messenger RNA, Intracellular Signaling Peptides and Proteins, RNA-Binding Proteins, hnRNPs, Recombinant Proteins, unclassified drug, Cross-Linking Reagents, priority journal, Ribonucleoproteins, ribonucleoprotein hrp1p, protein RNA binding, Hmt1p, Protein Binding, Molecular Sequence Data, RNA sequence, Polyadenylation, Arginine, Methylation, ribonucleoprotein, reverse transcription polymerase chain reaction, controlled study, Amino Acid Sequence, RNA, Messenger, protein methylation, Protein Processing, Cleavage, nonhuman, Binding Sites, Oligoribonucleotides, Base Sequence, binding site, cell nucleus, Post-Translational, DNA Helicases, RNA cleavage, Methyltransferases, RNA binding, RNA binding protein, Kinetics, RNA processing, RNA, methyltransferase, Protein Processing, Post-Translational
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