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EMBO J. Jun 1985; 4(6): 1609–1614.
PMCID: PMC554390

Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes.


The 7S particle of Xenopus laevis oocytes contains 5S RNA and a 40-K protein which is required for 5S RNA transcription in vitro. Proteolytic digestion of the protein in the particle yields periodic intermediates spaced at 3-K intervals and a limit digest containing 3-K fragments. The native particle is shown to contain 7-11 zinc atoms. These data suggest that the protein contains repetitive zinc-binding domains. Analysis of the amino acid sequence reveals nine tandem similar units, each consisting of approximately 30 residues and containing two invariant pairs of cysteines and histidines, the most common ligands for zinc. The linear arrangement of these repeated, independently folding domains, each centred on a zinc ion, comprises the major part of the protein. Such a structure explains how this small protein can bind to the long internal control region of the 5S RNA gene, and stay bound during the passage of an RNA polymerase molecule.

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Selected References

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  • Adman ET, Sieker LC, Jensen LH. Structure of a bacterial ferredoxin. J Biol Chem. 1973 Jun 10;248(11):3987–3996. [PubMed]
  • Bieker JJ, Martin PL, Roeder RG. Formation of a rate-limiting intermediate in 5S RNA gene transcription. Cell. 1985 Jan;40(1):119–127. [PubMed]
  • Bieker JJ, Roeder RG. Physical properties and DNA-binding stoichiometry of a 5 S gene-specific transcription factor. J Biol Chem. 1984 May 25;259(10):6158–6164. [PubMed]
  • Bogenhagen DF, Sakonju S, Brown DD. 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. [PubMed]
  • Bogenhagen DF, Wormington WM, Brown DD. Stable transcription complexes of Xenopus 5S RNA genes: a means to maintain the differentiated state. Cell. 1982 Feb;28(2):413–421. [PubMed]
  • Bolognesi M, Gatti G, Menagatti E, Guarneri M, Marquart M, Papamokos E, Huber R. Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation. J Mol Biol. 1982 Dec 25;162(4):839–868. [PubMed]
  • Boswell DR, McLachlan AD. Sequence comparison by exponentially-damped alignment. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 2):457–464. [PMC free article] [PubMed]
  • Boulanger Y, Goodman CM, Forte CP, Fesik SW, Armitage IM. Model for mammalian metallothionein structure. Proc Natl Acad Sci U S A. 1983 Mar;80(6):1501–1505. [PMC free article] [PubMed]
  • Ladiges WC, Raff RF, Brown S, Deeg HJ, Storb R. The canine major histocompatibility complex. Supertypic specificities defined by the primed lymphocyte test (PLT). Immunogenetics. 1984;19(4):359–365. [PubMed]
  • Cornell NW, Crivaro KE. Stability constant for the zinc-dithiothreitol complex. Anal Biochem. 1972 May;47(1):203–208. [PubMed]
  • Denis H, le Maire M. Thesaurisomes, a novel kind of nucleoprotein particle. Subcell Biochem. 1983;9:263–297. [PubMed]
  • Engelke DR, Ng SY, Shastry BS, Roeder RG. Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes. Cell. 1980 Mar;19(3):717–728. [PubMed]
  • Ginsberg AM, King BO, Roeder RG. 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):479–489. [PubMed]
  • Gottesfeld J, Bloomer LS. Assembly of transcriptionally active 5S RNA gene chromatin in vitro. Cell. 1982 Apr;28(4):781–791. [PubMed]
  • Honda BM, Roeder RG. Association of a 5S gene transcription factor with 5S RNA and altered levels of the factor during cell differentiation. Cell. 1980 Nov;22(1 Pt 1):119–126. [PubMed]
  • Hood L, Campbell JH, Elgin SC. The organization, expression, and evolution of antibody genes and other multigene families. Annu Rev Genet. 1975;9:305–353. [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Lassar AB, Martin PL, Roeder RG. Transcription of class III genes: formation of preinitiation complexes. Science. 1983 Nov 18;222(4625):740–748. [PubMed]
  • Lewis CD, Laemmli UK. Higher order metaphase chromosome structure: evidence for metalloprotein interactions. Cell. 1982 May;29(1):171–181. [PubMed]
  • McLachlan AD. Tests for comparing related amino-acid sequences. Cytochrome c and cytochrome c 551 . J Mol Biol. 1971 Oct 28;61(2):409–424. [PubMed]
  • McLachlan AD. Analysis of gene duplication repeats in the myosin rod. J Mol Biol. 1983 Sep 5;169(1):15–30. [PubMed]
  • Marshall RD. Glycoproteins. Annu Rev Biochem. 1972;41:673–702. [PubMed]
  • Moews PC, Kretsinger RH. Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis. J Mol Biol. 1975 Jan 15;91(2):201–225. [PubMed]
  • Needleman SB, Wunsch CD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol. 1970 Mar;48(3):443–453. [PubMed]
  • Ohlendorf DH, Matthews BW. Structural studies of protein-nucleic acid interactions. Annu Rev Biophys Bioeng. 1983;12:259–284. [PubMed]
  • Pelham HR, Brown DD. A specific transcription factor that can bind either the 5S RNA gene or 5S RNA. Proc Natl Acad Sci U S A. 1980 Jul;77(7):4170–4174. [PMC free article] [PubMed]
  • Picard B, Wegnez M. Isolation of a 7S particle from Xenopus laevis oocytes: a 5S RNA-protein complex. Proc Natl Acad Sci U S A. 1979 Jan;76(1):241–245. [PMC free article] [PubMed]
  • Rossmann MG, Argos P. Protein folding. Annu Rev Biochem. 1981;50:497–532. [PubMed]
  • Sakonju S, Bogenhagen DF, Brown DD. 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. [PubMed]
  • Segall J, Matsui T, Roeder RG. Multiple factors are required for the accurate transcription of purified genes by RNA polymerase III. J Biol Chem. 1980 Dec 25;255(24):11986–11991. [PubMed]
  • Smith DR, Jackson IJ, Brown DD. Domains of the positive transcription factor specific for the Xenopus 5S RNA gene. Cell. 1984 Jun;37(2):645–652. [PubMed]

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