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J. Biol. Chem., Vol. 259, Issue 18, 11373-11382, 09, 1984
BS Shastry, BM Honda and RG Roeder
Xenopus laevis oocytes contain a 38,000-Da protein which serves both as a 5 S gene-specific transcription initiation factor (TFIIIA) and to stabilize 5 S RNA in ribonucleoprotein complexes. Using an antibody to this protein we have measured the levels of TFIIIA during oogenesis and embryonic development in X. laevis. The maximal steady state level (approximately 10(12) molecules/oocyte) is reached early in oogenesis but drops 10- to 20-fold in later stages and another 10- to 20-fold during ovulation. The reduced amount present in the unfertilized egg remains at a nearly constant level throughout early development, but with cell division the cellular concentration drops from 3 X 10(9) to about 10(4) molecules/cell. An immunoreactive protein of the same size is also found in liver tissues and in cultured kidney cells, which also contain about 10(4) molecules/cell. By both structural (CNBr peptide analysis) and functional (transcription of 5 S genes) analyses the embryonic and kidney cell 38,000-Da factors appear indistinguishable from oocyte TFIIIA. In addition a second antigenically related protein of about 40,000 Da is found in late stage embryos, liver tissues, and adult kidney cells (where it is severalfold more abundant than the 38,000-Da TFIIIA). The chromatographic fractionation and functional analysis of the kidney cell extracts has shown that fractions containing the 38,000-Da protein support 5 S RNA synthesis while fractions containing the 40,000-Da protein do not. The significance of these findings for 5 S gene regulation is discussed with respect to the dual function of TFIIIA, the presence of rate-limiting amounts of TFIIIA, and the possibility of stage-specific factors.
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  R. Ghose, M. Malik, and P. W. Huber Restricted Specificity of Xenopus TFIIIA for Transcription of Somatic 5S rRNA Genes Mol. Cell. Biol., March 15, 2004; 24(6): 2467 - 2477. [Abstract] [Full Text] [PDF]
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L. Howe and J. Ausió Nucleosome Translational Position, Not Histone Acetylation, Determines TFIIIA Binding to Nucleosomal Xenopus laevis 5S rRNA Genes Mol. Cell. Biol., March 1, 1998; 18(3): 1156 - 1162. [Abstract] [Full Text]
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 P Bouvet, S Dimitrov, and A P Wolffe Specific regulation of Xenopus chromosomal 5S rRNA gene transcription in vivo by histone H1. Genes & Dev., May 15, 1994; 8(10): 1147 - 1159. [Abstract] [PDF]
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S H Kim, M K Darby, K E Joho, and D D Brown The characterization of the TFIIIA synthesized in somatic cells of Xenopus laevis. Genes & Dev., September 1, 1990; 4(9): 1602 - 1610. [Abstract] [PDF]
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J Blanco, L Millstein, M A Razik, S Dilworth, C Cote, and J Gottesfeld Two TFIIIA activities regulate expression of the Xenopus 5S RNA gene families. Genes & Dev., October 1, 1989; 3(10): 1602 - 1612. [Abstract] [PDF]
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K W Scotto, H Kaulen, and R G Roeder Positive and negative regulation of the gene for transcription factor IIIA in Xenopus laevis oocytes. Genes & Dev., May 1, 1989; 3(5): 651 - 662. [Abstract] [PDF]
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G A McConkey and D F Bogenhagen TFIIIA binds with equal affinity to somatic and major oocyte 5S RNA genes. Genes & Dev., February 1, 1988; 2(2): 205 - 214. [Abstract] [PDF]
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E Lund, C J Bostock, and J E Dahlberg The transcription of Xenopus laevis embryonic U1 snRNA genes changes when oocytes mature into eggs. Genes & Dev., March 1, 1987; 1(1): 47 - 56. [Abstract] [PDF]
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