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Xenopus transcription factor, termed TFIIIA, is the first eukaryotic transcription factor purified to homogeneity and one of the most extensively characterized polymerase III gene factors at the levels both of the protein and its gene. It is an abundant protein in oocytes and is specifically required for the 5S RNA gene transcription. It promotes the formation of a stable transcription complex by first binding to the internal control region of the 5S RNA gene through its zinc finger motifs. It contains two structural domains and associates with 5S RNA to form 7S ribonucleoprotein particles in oocytes. Its expression is developmentally controlled at the level of transcription and translation. It participates in the assembly of active chromatin templates and, at least in part, is responsible for the differential expression of two kinds of 5S RNA genes in Xenopus.
Allison,
RNA-protein interactions of stored 5S RNA with TFIIIA and ribosomal protein L5 during Xenopus oogenesis.
1991, Pubmed,
Xenbase
Allison,
RNA-protein interactions of stored 5S RNA with TFIIIA and ribosomal protein L5 during Xenopus oogenesis.
1991,
Pubmed
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Xenbase
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The deduced sequence of the transcription factor TFIIIA from Saccharomyces cerevisiae reveals extensive divergence from Xenopus TFIIIA.
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Xenbase
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Two TFIIIA activities regulate expression of the Xenopus 5S RNA gene families.
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Pubmed
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Xenbase
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Binding of TFIIIA to derivatives of 5S RNA containing sequence substitutions or deletions defines a minimal TFIIIA binding site.
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Pubmed
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Xenbase
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Xenbase
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Displacement of Xenopus transcription factor IIIA from a 5S rRNA gene by a transcribing RNA polymerase.
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Xenbase
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Sequence-specific binding of the N-terminal three-finger fragment of Xenopus transcription factor IIIA to the internal control region of a 5S RNA gene.
1991,
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Xenbase
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Molecular basis for specific recognition of both RNA and DNA by a zinc finger protein.
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Xenbase
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Definition of the binding sites of individual zinc fingers in the transcription factor IIIA-5S RNA gene complex.
1992,
Pubmed
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Xenbase
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Differential binding of zinc fingers from Xenopus TFIIIA and p43 to 5S RNA and the 5S RNA gene.
1992,
Pubmed
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Xenbase
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The use of chemical nucleases to analyze RNA-protein interactions. The TFIIIA-5 S rRNA complex.
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Xenbase
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Xenbase
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Xenbase
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Xenbase
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Structure of the TFIIIA-5 S DNA complex.
1992,
Pubmed
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Xenbase
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Xenbase
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Xenbase
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A finger protein structurally similar to TFIIIA that binds exclusively to 5S RNA in Xenopus.
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1991,
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Xenbase
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Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5 S RNA gene.
1992,
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Xenbase
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Pubmed
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Pubmed
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Xenbase
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Regulation of the Xenopus laevis transcription factor IIIA gene during oogenesis and early embryogenesis: negative elements repress the O-TFIIIA promoter in embryonic cells.
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Xenbase
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Characterization of a Xenopus oocyte factor that binds to a developmentally regulated cis-element in the TFIIIA gene.
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Xenbase
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The carboxyterminal zinc fingers of TFIIIA interact with the tip of helix V of 5S RNA in the 7S ribonucleoprotein particle.
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Xenbase
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Two zinc finger proteins from Xenopus laevis bind the same region of 5S RNA but with different nuclease protection patterns.
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Xenbase
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Pubmed
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Xenopus transcription factor IIIC (TFIIIC) specifically interacts with the "B" block region of the TFIIIA gene.
1991,
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Xenbase
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Yeast TFIIIA + TFIIIC/tau-factor, but not yeast TFIIIA alone, interacts with the Xenopus 5S rRNA gene.
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Xenbase
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Xenbase
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1988,
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Xenbase
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Pubmed
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Xenbase
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Zinc transfer from transcription factor IIIA fingers to thionein clusters.
1991,
Pubmed
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Xenbase
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