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PMID: 2164687 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 14 ·1990-07-00 ·Pages 5528-32

Churchill ME, Tullius TD, Klug A

Abstract

The zinc finger protein TFIIIA, a positive transcription factor of the 5S RNA gene, binds to an internal control region of 50 nucleotides. Two modes of binding have been considered for the TFIIIA-DNA complex, one of which has been proposed on the basis of nuclease and chemical protection experiments and the other on model building. Since then, evidence has accumulated on the structures of individual components of the complex--for example, zinc finger polypeptides studied by NMR and a segment of the binding site analyzed by x-ray crystallography, but no high-resolution structural data on the TFIIIA-DNA complex itself are available. Probes used previously to study the TFIIIA-DNA complex do not react with every nucleotide of DNA, unlike hydroxyl radical, which cleaves DNA at every backbone position. We describe here the quantitative analysis of high-resolution hydroxyl radical footprints and suggest how the array of zinc fingers might interact with the double helix.

MeSH Terms
Animals DNA, Ribosomal/genetics,metabolism DNA-Binding Proteins/metabolism Free Radicals Genes Hydroxides/analysis Hydroxyl Radical Magnetic Resonance Spectroscopy Metalloproteins/metabolism Models, Structural Nucleic Acid Conformation Protein Binding Protein Conformation RNA, Ribosomal/genetics RNA, Ribosomal, 5S/genetics Transcription Factor TFIIIA Transcription Factors/metabolism X-Ray Diffraction Xenopus Zinc/metabolism
Chemicals
DNA, Ribosomal DNA-Binding Proteins Free Radicals Hydroxides Metalloproteins RNA, Ribosomal RNA, Ribosomal, 5S Transcription Factor TFIIIA Transcription Factors Hydroxyl Radical Zinc
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Churchill M E
Medical Research Council Laboratory of Molecular Biology, Cambridge, England.
Tullius T D
Klug A
References (33)
33 references, click to expand
  1. Point mutational analysis of the Xenopus laevis 5S gene promoter.
    EMBO J. 1985 Jul;4(7):1847-53 PMID: 2992947
  2. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes.
    EMBO J. 1985 Jun;4(6):1609-14 PMID: 4040853
  3. An underlying repeat in some transcriptional control sequences corresponding to half a double helical turn of DNA.
    Cell. 1986 Jul 4;46(1):123-32 PMID: 3013416
  4. Hydroxyl radical "footprinting": high-resolution information about DNA-protein contacts and application to lambda repressor and Cro protein.
    Proc Natl Acad Sci U S A. 1986 Aug;83(15):5469-73 PMID: 3090544
  5. The crystal structure of d(GGATGGGAG): an essential part of the binding site for transcription factor IIIA.
    Nature. 1986 Aug 14-20;322(6080):661-4 PMID: 3748146
  6. Mapping of the sites of protection on a 5 S RNA gene by the Xenopus transcription factor IIIA. A model for the interaction.
    J Mol Biol. 1986 Dec 5;192(3):577-91 PMID: 3560227
  7. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain.
    Cell. 1987 Dec 24;51(6):1079-90 PMID: 3319186
  8. Hydroxyl radical footprinting: a high-resolution method for mapping protein-DNA contacts.
    Methods Enzymol. 1987;155:537-58 PMID: 2828876
  9. Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins.
    Proc Natl Acad Sci U S A. 1988 Jan;85(1):99-102 PMID: 3124104
  10. Mapping functional regions of transcription factor TFIIIA.
    Mol Cell Biol. 1988 Apr;8(4):1684-96 PMID: 2837652
  11. A Holliday recombination intermediate is twofold symmetric.
    Proc Natl Acad Sci U S A. 1988 Jul;85(13):4653-6 PMID: 3387432
  12. Zinc-dependent structure of a single-finger domain of yeast ADR1.
    Science. 1988 Sep 16;241(4872):1489-92 PMID: 3047872
  13. The helix-turn-helix DNA binding motif.
    J Biol Chem. 1989 Feb 5;264(4):1903-6 PMID: 2644244
  14. A model for the tertiary structure of the 28 residue DNA-binding motif ('zinc finger') common to many eukaryotic transcriptional regulatory proteins.
    Protein Eng. 1988 Sep;2(3):209-18 PMID: 3148934
  15. Physical studies of protein-DNA complexes by footprinting.
    Annu Rev Biophys Biophys Chem. 1989;18:213-37 PMID: 2660824
  16. Transcription factor IIIA induced bending of the Xenopus somatic 5S gene promoter.
    Nature. 1989 Aug 10;340(6233):487-8 PMID: 2755511
  17. Three-dimensional solution structure of a single zinc finger DNA-binding domain.
    Science. 1989 Aug 11;245(4918):635-7 PMID: 2503871
  18. A novel method for the purification of the Xenopus transcription factor IIIA.
    Nucleic Acids Res. 1989 Nov 25;17(22):9185-92 PMID: 2511557
  19. Sequence-specific [1H]NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
    FEBS Lett. 1990 Mar 26;262(2):179-84 PMID: 2110530
  20. Kinetic analysis of deoxyribonuclease I cleavages in the nucleosome core: evidence for a DNA superhelix.
    J Mol Biol. 1978 Sep 15;124(2):391-420 PMID: 568667
  21. A control region in the center of the 5S RNA gene directs specific initiation of transcription: I. The 5' border of the region.
    Cell. 1980 Jan;19(1):13-25 PMID: 7357599
  22. A control region in the center of the 5S RNA gene directs specific initiation of transcription: II. The 3' border of the region.
    Cell. 1980 Jan;19(1):27-35 PMID: 7357604
  23. Helical periodicity of DNA determined by enzyme digestion.
    Nature. 1980 Aug 7;286(5773):573-8 PMID: 7402337
  24. The binding of a transcription factor to deletion mutants of a 5S ribosomal RNA gene.
    Cell. 1981 Mar;23(3):665-9 PMID: 7226225
  25. Map of distamycin, netropsin, and actinomycin binding sites on heterogeneous DNA: DNA cleavage-inhibition patterns with methidiumpropyl-EDTA.Fe(II).
    Proc Natl Acad Sci U S A. 1982 Sep;79(18):5470-4 PMID: 6291045
  26. Contact points between a positive transcription factor and the Xenopus 5S RNA gene.
    Cell. 1982 Dec;31(2 Pt 1):395-405 PMID: 6297765
  27. The role of stable complexes that repress and activate eucaryotic genes.
    Cell. 1984 Jun;37(2):359-65 PMID: 6722879
  28. Domains of the positive transcription factor specific for the Xenopus 5S RNA gene.
    Cell. 1984 Jun;37(2):645-52 PMID: 6722885
  29. Structural specificities of five commonly used DNA nucleases.
    J Mol Biol. 1984 Jul 15;176(4):535-57 PMID: 6086935
  30. Multiple specific contacts between a mammalian transcription factor and its cognate promoters.
    Nature. 1984 Nov 29-Dec 5;312(5993):409-13 PMID: 6095100
  31. Xenopus 5S gene transcription factor, TFIIIA: characterization of a cDNA clone and measurement of RNA levels throughout development.
    Cell. 1984 Dec;39(3 Pt 2):479-89 PMID: 6210149
  32. The primary structure of transcription factor TFIIIA has 12 consecutive repeats.
    FEBS Lett. 1985 Jul 8;186(2):271-4 PMID: 4007166
  33. Structural analysis of a triple complex between the histone octamer, a Xenopus gene for 5S RNA and transcription factor IIIA.
    EMBO J. 1985 Dec 16;4(13A):3473-82 PMID: 4092686
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.87.14.5528
Published
1990-07-00
Pages
5528-32
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC54358
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.87.14.5528 PMC Full Text View journal details
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