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PMID: 1380452 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Interaction of the RNA-binding domain of the hnRNP C proteins with RNA.

The EMBO journal ·Vol. 11 ·No. 9 ·1992-09-00 ·Pages 3289-95

Görlach M, Wittekind M, Beckman RA, Mueller L, Dreyfuss G

Abstract

The hnRNP C proteins are among the most abundant and avid pre-mRNA-binding proteins and they contain a consensus sequence RNA-binding domain (RBD) that is found in a large number of RNA-binding proteins. The interaction of the RBD of the hnRNP C proteins with an RNA oligonucleotide [r(U)8] was monitored by nuclear magnetic resonance (NMR). 15N and 13C/15N-labelled hnRNP C protein RBD was mixed with r(U)8 and one- and two-dimensional (1D and 2D) NMR spectra were recorded in a titration experiment. NMR studies of the uncomplexed 93 amino acid hnRNP C RBD (Wittekind et al., 1992) have shown that it has a compact folded structure (beta alpha beta beta alpha beta), which is typical for the RBD of this family of proteins and which is comprised of a four-stranded antiparallel beta-sheet, two alpha-helices and relatively unstructured amino- and carboxy-terminal regions. Sequential assignments of the polypeptide main-chain atoms of the hnRNP C RBD-r(U)8 complex revealed that these typical structural features are maintained in the complex, but significant perturbations of the chemical shifts of amide group atoms occur in a large number of residues. Most of these residues are in the beta-sheet region and especially in the terminal regions of the RBD. In contrast; chemical shifts of the residues of the well conserved alpha-helices, with the exception of Lys30, are not significantly perturbed. These observations localize the candidate residues of the RBD that are involved in the interaction with the RNA.(ABSTRACT TRUNCATED AT 250 WORDS)

MeSH Terms
Amino Acid Sequence Binding Sites Escherichia coli/genetics Heterogeneous-Nuclear Ribonucleoprotein Group C Heterogeneous-Nuclear Ribonucleoproteins Humans Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Protein Conformation RNA/metabolism RNA Precursors/metabolism RNA-Binding Proteins/chemistry,metabolism Recombinant Proteins/chemistry,metabolism Ribonucleoproteins/chemistry,metabolism
Chemicals
Heterogeneous-Nuclear Ribonucleoprotein Group C Heterogeneous-Nuclear Ribonucleoproteins RNA Precursors RNA-Binding Proteins Recombinant Proteins Ribonucleoproteins RNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Görlach M
Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6148.
Wittekind M
Beckman R A
Mueller L
Dreyfuss G
References (36)
36 references, click to expand
  1. A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein.
    Cell. 1989 Apr 7;57(1):89-101 PMID: 2467746
  2. Autoregulation of gene expression. Quantitative evaluation of the expression and function of the bacteriophage T4 gene 32 (single-stranded DNA binding) protein system.
    J Mol Biol. 1982 Dec 25;162(4):795-818 PMID: 6984860
  3. Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts.
    Proc Natl Acad Sci U S A. 1989 Dec;86(24):9788-92 PMID: 2557628
  4. Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein.
    J Biol Chem. 1988 Mar 5;263(7):3307-13 PMID: 2830282
  5. Structure of rodent helix-destabilizing protein revealed by cDNA cloning.
    J Biol Chem. 1986 Mar 15;261(8):3536-43 PMID: 3005291
  6. Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins.
    Genes Dev. 1988 Feb;2(2):215-27 PMID: 3129338
  7. Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities.
    Mol Cell Biol. 1988 May;8(5):2237-41 PMID: 3386636
  8. Heterogeneous nuclear ribonucleoproteins: role in RNA splicing.
    Science. 1986 Mar 28;231(4745):1534-9 PMID: 3952495
  9. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.
    Mol Cell Biol. 1991 Jul;11(7):3419-24 PMID: 1675426
  10. Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions.
    Cell. 1991 Nov 1;67(3):517-28 PMID: 1682054
  11. A uridylate tract mediates efficient heterogeneous nuclear ribonucleoprotein C protein-RNA cross-linking and functionally substitutes for the downstream element of the polyadenylation signal.
    Mol Cell Biol. 1990 Dec;10(12):6397-407 PMID: 1701018
  12. RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
    Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2495-9 PMID: 1826055
  13. Identification of molecular contacts between the U1 A small nuclear ribonucleoprotein and U1 RNA.
    EMBO J. 1991 Nov;10(11):3447-56 PMID: 1833186
  14. Protein--DNA contacts in the structure of a homeodomain--DNA complex determined by nuclear magnetic resonance spectroscopy in solution.
    EMBO J. 1990 Oct;9(10):3085-92 PMID: 1976507
  15. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A.
    Nature. 1990 Dec 6;348(6301):515-20 PMID: 2147232
  16. The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation.
    Cell. 1990 Mar 9;60(5):733-46 PMID: 2155707
  17. The Xenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains.
    EMBO J. 1990 Nov;9(11):3699-705 PMID: 2209558
  18. Design of DNA-binding peptides based on the leucine zipper motif.
    Science. 1990 Aug 17;249(4970):774-8 PMID: 2389143
  19. RNA-binding proteins as developmental regulators.
    Genes Dev. 1989 Apr;3(4):431-7 PMID: 2470643
  20. Common structural changes accompany the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution.
    Biochemistry. 1989 Dec 26;28(26):9908-12 PMID: 2515891
  21. Molecular characterization of helix-loop-helix peptides.
    Science. 1992 Feb 21;255(5047):979-83 PMID: 1312255
  22. Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA.
    Proc Natl Acad Sci U S A. 1990 Aug;87(16):6393-7 PMID: 1696729
  23. RNA recognition: towards identifying determinants of specificity.
    Trends Biochem Sci. 1991 Jun;16(6):214-20 PMID: 1716386
  24. A structural taxonomy of DNA-binding domains.
    Nature. 1991 Oct 24;353(6346):715-9 PMID: 1944532
  25. Major determinants of the specificity of interaction between small nuclear ribonucleoproteins U1A and U2B'' and their cognate RNAs.
    Nature. 1990 Jun 7;345(6275):502-6 PMID: 2140872
  26. Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding.
    Q Rev Biophys. 1990 Aug;23(3):205-80 PMID: 2204954
  27. Recombinant hnRNP protein A1 and its N-terminal domain show preferential affinity for oligodeoxynucleotides homologous to intron/exon acceptor sites.
    Nucleic Acids Res. 1990 Nov 25;18(22):6595-600 PMID: 2251120
  28. Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA.
    EMBO J. 1989 Dec 20;8(13):4163-70 PMID: 2531658
  29. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta.
    Biochemistry. 1989 Jul 25;28(15):6150-6 PMID: 2675964
  30. Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a.
    Biochemistry. 1989 Mar 21;28(6):2387-91 PMID: 2730871
  31. The C proteins of heterogeneous nuclear ribonucleoprotein complexes interact with RNA sequences downstream of polyadenylation cleavage sites.
    Mol Cell Biol. 1988 Oct;8(10):4477-83 PMID: 2847033
  32. Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation.
    Trends Biochem Sci. 1988 Mar;13(3):86-91 PMID: 3072706
  33. Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions.
    Science. 1988 Nov 11;242(4880):893-9 PMID: 3187530
  34. RNA binding specificity of hnRNP proteins: a subset bind to the 3' end of introns.
    EMBO J. 1988 Nov;7(11):3519-29 PMID: 3208740
  35. Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins.
    J Biol Chem. 1986 Aug 25;261(24):11266-73 PMID: 3733753
  36. A binding consensus: RNA-protein interactions in splicing, snRNPs, and sex.
    Cell. 1989 Apr 7;57(1):1-3 PMID: 2522817
Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1992-09-00
Pages
3289-95
Language
English
Region
England
NLM ID
8208664
PMCID
PMC556863
Subset
IM
Grants
NCI NIH HHS · 1K11CA01456-02 · United States
External Links
PubMed source PMC Full Text View journal details
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