Unusual Sites of Arginine Methylation in Poly(A)-binding Protein II and in Vitro Methylation by Protein Arginine Methyltransferases PRMT1 and PRMT3*
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Summary
Poly(A)-binding protein II and deletion mutants expressed in Escherichia coli were in vitro substrates for two mammalian protein arginine methyltransferases, PRMT1 and PRMT3, withS-adenosyl-l-methionine as the methyl group donor.
- Type
- article
- Published
- 1999-05-07
- Cited by
- 150
- References
- 48
- Access
- Open access
- OpenAlex
- https://openalex.org/W2003083382
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:21618729
Keywords
Methylation, Methyltransferase, Arginine, Protein methylation, Biochemistry
References
- Arginine methylation facilitates the nuclear export of hnRNP proteins.
- PRMT 3, a Type I Protein Arginine N-Methyltransferase That Differs from PRMT1 in Its Oligomerization, Subcellular Localization, Substrate Specificity, and Regulation*
- Assembly of a processive messenger RNA polyadenylation complex.
- RNA and protein interactions modulated by protein arginine methylation.
- Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases.
- Primary structure of rat ribosomal protein S2. A ribosomal protein with arginine-glycine tandem repeats and RGGF motifs that are associated with nucleolar localization and binding to ribonucleic acids.
- Nucleolar specific acidic phosphoprotein C23 is highly methylated.
- The UUAG-specific RNA Binding Protein, Heterogeneous Nuclear Ribonucleoprotein D0
- Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine.
- Mammalian poly(A)-binding protein II. Physical properties and binding to polynucleotides.
- Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box.
- Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins.
- Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase.
- Conserved structures and diversity of functions of RNA-binding proteins.
- Concerted activities of the RNA recognition and the glycine-rich C-terminal domains of nucleolin are required for efficient complex formation with pre-ribosomal RNA.
- Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe is a preferred recognition motif.
- Substrate specificity for myelin basic protein-specific protein methylase I.
- Nuclear RNA export.
- hnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins.
- Structural specificity of substrate for S-adenosylmethionine:protein arginine N-methyltransferases.
Cited by
- Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why
- Protein arginine methylation in health and disease.
- Post-translational modification of delta antigen of hepatitis D virus.
- Role of HSWI/SNF associated PRMT5 and MSIN3A/HDAC in the control of gene expression and cancer.
- Caractérisation de la diversité épigénétique chez différentes espèces cultivées et sauvages de tomate
- The characterization of inner core protein VP6 of African horsesickness virus
- The RNA Binding Domains of the Nuclear poly(A)-binding Protein* 210
- Lean forward: Genetic analysis of temperature-sensitive mutants unfolds the secrets of oligomeric protein complex assembly
- A Proline‐Tyrosine Nuclear Localization Signal (PY‐NLS) Is Required for the Nuclear Import of Fission Yeast PAB2, but Not of Human PABPN1
- Role of the Adenovirus Type 5 L4-100K Protein During Lytic Infection
- Interferon alpha signaling in viral hepatitis
- 3 Diverse roles of protein arginine methyltransferases.
- Differential gene expression screening uncovers downregulation of the cell cycle regulator BTG2 as an important step in renal tumor biology
- THE HNRNP F AND HNRNP H' AREMAMMALIAN 3' MRNA PROCESSING FACTORS ACTING THROUGH GUANINE RICH SEQUENCES
- 4 Structure of protein arginine methyltransferases.
- Poly(A) RNA Binding Proteins and Polyadenosine RNA: New Members and Novel Functions
- The predominant protein arginine methyltransferase PRMT1 is critical for zebrafish convergence and extension during gastrulation
- Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1.
- Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts its phosphorylation and inactivation by Akt
- Nerve growth factor‐mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1
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