scholarly journals Transcription Factor IIIB 90 kDa Subunit

2020 ◽  
Author(s):  
Keyword(s):  
Transcription Factor ◽  
Transcription Factor Iiib

scholarly journals Purification of transcription factor IIIB from HeLa cells.

1988 ◽  
Vol 263 (26) ◽  
pp. 13350-13356 ◽  
Author(s):  
R Waldschmidt ◽  
D Jahn ◽  
K H Seifart
Keyword(s):  
Transcription Factor ◽  
Hela Cells ◽  
Transcription Factor Iiib

Identical components of yeast transcription factor IIIB are required and sufficient for transcription of TATA box-containing and TATA-less genes

1994 ◽  
Vol 14 (4) ◽  
pp. 2798-2808
Author(s):  
C A Joazeiro ◽  
G A Kassavetis ◽  
E P Geiduschek
Keyword(s):  
Transcription Factor ◽  
Protein Interactions ◽  
Rna Polymerase Iii ◽  
5S Rdna ◽  
Tata Box ◽  
Trna Genes ◽  
Small Nuclear Rna ◽  
Protein Protein Interactions ◽  
Tata Element ◽  
Transcription Factor Iiib

Specific transcription by RNA polymerase III requires recognition of the promoter-bound transcription factor IIIB (TFIIIB), of which the TATA-binding protein (TBP) is a subunit. The recruitment of TFIIIB to TATA-less genes is mediated by protein-protein interactions with transcription factor IIIC (TFIIIC) bound to the box A and box B elements. Here we examine interactions involved in the recruitment of TFIIIB to the TATA element-containing yeast U6 small nuclear RNA gene SNR6. TFIIIC is not required for the formation of TFIIIB-SNR6 gene complexes with purified components. The same three components of TFIIIB that are necessary for TFIIIC-dependent transcription of tRNA genes (recombinant TBP and Brf and the denaturing-gel-purified 90-kDa subunit) are required and sufficient for TATA box-directed U6 transcription. Despite its TFIIIC-independent, DNA sequence-dependent assembly, the TFIIIB-SNR6 complex shares important features with tDNA- and 5S rDNA-TFIIIB complexes, such as extent and location of footprint, stability, and resistance to heparin. These properties are clearly distinct from those of a TBP-SNR6 complex. In the SNR6 gene, box B, the primary binding site for TFIIIC, is suboptimally spaced relative to box A. At limiting TBP concentrations and on bare DNA, TFIIIC stimulates the formation of TFIIIB complexes with SNR6 but contributes poorly, at best, to the formation of properly placed complexes.

scholarly journals Alignment of the B" Subunit of RNA Polymerase III Transcription Factor IIIB in Its Promoter Complex

1999 ◽  
Vol 274 (40) ◽  
pp. 28736-28744 ◽  
Author(s):  
Sheila M. A. Shah ◽  
Ashok Kumar ◽  
E. Peter Geiduschek ◽  
George A. Kassavetis
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Iii ◽  
B Subunit ◽  
Polymerase Iii ◽  
Promoter Complex ◽  
Transcription Factor Iiib

scholarly journals Domains of the Brf component of RNA polymerase III transcription factor IIIB (TFIIIB): functions in assembly of TFIIIB-DNA complexes and recruitment of RNA polymerase to the promoter.

1997 ◽  
Vol 17 (9) ◽  
pp. 5299-5306 ◽  
Author(s):  
G A Kassavetis ◽  
C Bardeleben ◽  
A Kumar ◽  
E Ramirez ◽  
E P Geiduschek
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Binding Protein ◽  
Rna Polymerase Iii ◽  
Tata Binding Protein ◽  
Terminal Segment ◽  
Dna Complexes ◽  
Polymerase Iii ◽  
Transcription Factor Iiib ◽  
Derivatives Of

Saccharomyces cerevisiae transcription factor IIIB (TFIIIB) is composed of three subunits: the TATA-binding protein, the TFIIB-related protein Brf, and B". TFIIIB, which is brought to RNA polymerase III-transcribed genes indirectly through interaction with DNA-bound TFIIIC or directly through DNA recognition by the TATA-binding protein, in turn recruits RNA polymerase III to the promoter. N-terminally deleted derivatives of Brf have been examined for their ability to interact with DNA-bound TFIIIC and with the other components of TFIIIB and for participation in transcription. Brf(165-596), lacking 164 N-proximal TFIIB-homologous amino acids, is competent to participate in the assembly of TFIIIB-DNA complexes and in TFIIIC-independent transcription. Even deletion of the entire TFIIB-homologous half of the protein, as in Brf(317-596) and Brf(352-596), allows some interaction with DNA-bound TBP and with the B" component of TFIIIB to be retained. The function of Brf(165-596) in transcription has also been examined in the context of B" with small internal deletions. The ability of Brf with this sizable N-terminal segment deleted to function in TFIIIC-independent transcription requires segments of B" that are individually indispensable although required on an either/or basis, in the context of complete Brf. These findings suggest a functional complementarity and reciprocity between the Brf and B" components of TFIIIB.

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