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PMID: 1826055 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 6 ·1991-03-15 ·Pages 2495-9

Hoffman DW, Query CC, Golden BL, White SW, Keene JD

Abstract

An RNA recognition motif (RRM) of approximately 80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human U1 small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel beta-strands and two alpha-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent beta-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.

MeSH Terms

Amino Acid Sequence Binding Sites Escherichia coli/genetics Magnetic Resonance Spectroscopy/methods Models, Molecular Molecular Sequence Data Protein Conformation RNA, Small Nuclear/metabolism Recombinant Proteins/chemistry,metabolism Ribonucleoproteins/chemistry,metabolism Ribonucleoproteins, Small Nuclear Ribosomal Proteins/chemistry,metabolism Sequence Homology, Nucleic Acid

Chemicals

RNA, Small Nuclear Recombinant Proteins Ribonucleoproteins Ribonucleoproteins, Small Nuclear Ribosomal Proteins

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Hoffman D W

Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.

Query C C

Golden B L

White S W

Keene J D

References (32)

32 references, click to expand

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
A method for multiple sequence alignment with gaps.
J Mol Biol. 1989 Oct 20;209(4):539-48 PMID: 2685324
A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability.
Mol Cell Biol. 1987 Sep;7(9):3268-76 PMID: 3313012
Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A.
J Mol Biol. 1987 Jun 5;195(3):555-79 PMID: 3309338
Sequence comparison of single-stranded DNA binding proteins and its structural implications.
J Mol Biol. 1987 Feb 5;193(3):579-84 PMID: 3295261
mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence.
Mol Cell Biol. 1986 Aug;6(8):2932-43 PMID: 3537727
Crystal structure of a prokaryotic ribosomal protein.
Proc Natl Acad Sci U S A. 1986 Oct;83(19):7251-5 PMID: 3463963
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
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
DNA recognition by proteins with the helix-turn-helix motif.
Annu Rev Biochem. 1990;59:933-69 PMID: 2197994
Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif.
EMBO J. 1990 Sep;9(9):2783-90 PMID: 2390971
The anatomy and taxonomy of protein structure.
Adv Protein Chem. 1981;34:167-339 PMID: 7020376
Mechanism of DNA binding to the gene 5 protein of bacteriophage fd.
Biochemistry. 1984 Jan 17;23(2):340-9 PMID: 6365163
On the use of chemically derived distance constraints in the prediction of protein structure with myoglobin as an example.
J Mol Biol. 1980 Feb 15;137(1):9-22 PMID: 7365797
On the conformation of proteins: the handedness of the connection between parallel beta-strands.
J Mol Biol. 1977 Feb 25;110(2):269-83 PMID: 845952
Handedness of crossover connections in beta sheets.
Proc Natl Acad Sci U S A. 1976 Aug;73(8):2619-23 PMID: 183204
Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Biochemistry. 1990 Jul 10;29(27):6341-62 PMID: 2207079
Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy.
J Mol Biol. 1989 May 20;207(2):405-15 PMID: 2547076
Zinc-dependent structure of a single-finger domain of yeast ADR1.
Science. 1988 Sep 16;241(4872):1489-92 PMID: 3047872
Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignments.
Biochemistry. 1986 Nov 18;25(23):7760-9 PMID: 3542034
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
Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution.
Science. 1989 Dec 1;246(4934):1135-42 PMID: 2479982
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.
Gene. 1988 Jul 15;67(1):31-40 PMID: 3047011
cDNA cloning of the human U1 snRNA-associated A protein: extensive homology between U1 and U2 snRNP-specific proteins.
EMBO J. 1987 Dec 1;6(12):3841-8 PMID: 2962859
Sex-lethal, a Drosophila sex determination switch gene, exhibits sex-specific RNA splicing and sequence similarity to RNA binding proteins.
Cell. 1988 Dec 23;55(6):1037-46 PMID: 3144435
Structural comparison of the prokaryotic ribosomal proteins L7/L12 and L30.
Proteins. 1988;3(4):243-51 PMID: 3047743
Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation.
Trends Biochem Sci. 1988 Mar;13(3):86-91 PMID: 3072706
Secondary structure prediction for RNA binding domain in RNP proteins identifies beta alpha beta as the main structural motif.
FEBS Lett. 1989 Nov 6;257(2):373-6 PMID: 2479579
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
RNA-binding proteins as developmental regulators.
Genes Dev. 1989 Apr;3(4):431-7 PMID: 2470643
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
The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation.
Cell. 1989 Sep 8;58(5):857-67 PMID: 2673535

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.88.6.2495

Published

1991-03-15

Pages

2495-9

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC51259

Subset

Grants

NIGMS NIH HHS · GM07184 · United States

External Links

PubMed source DOI: 10.1073/pnas.88.6.2495 PMC Full Text View journal details

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RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.

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