scholarly journals Functional interaction of the subunit 3 of RNA polymerase II (RPB3) with transcription factor-4 (ATF4)

FEBS Letters ◽  
2003 ◽  
Vol 547 (1-3) ◽  
pp. 15-19 ◽  
Author(s):  
Roberta De Angelis ◽  
Simona Iezzi ◽  
Tiziana Bruno ◽  
Nicoletta Corbi ◽  
Monica Di Padova ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Functional Interaction ◽  
Transcription Factor 4

Modulation of RNA polymerase core functions by basal transcription factor TFB/TFIIB

2006 ◽  
Vol 73 ◽  
pp. 49-58 ◽  
Author(s):  
Finn Werner ◽  
Simone Wiesler ◽  
Sven Nottebaum ◽  
Robert O.J. Weinzierl
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Bioinformatics Analysis ◽  
Functional Interaction ◽  
Basal Transcription ◽  
Basal Transcriptional Machinery ◽  
Functional Implications ◽  
Systematic Evolution ◽  
Basal Transcription Factors

The archaeal basal transcriptional machinery consists of TBP (TATA-binding protein), TFB (transcription factor B; a homologue of eukaryotic TFIIB) and an RNA polymerase that is structurally very similar to eukaryotic RNA polymerase II. This constellation of factors is sufficient to assemble specifically on a TATA box-containing promoter and to initiate transcription at a specific start site. We have used this system to study the functional interaction between basal transcription factors and RNA polymerase, with special emphasis on the post-recruitment function of TFB. A bioinformatics analysis of the B-finger of archaeal TFB and eukaryotic TFIIB reveals that this structure undergoes rapid and apparently systematic evolution in archaeal and eukaryotic evolutionary domains. We provide a detailed analysis of these changes and discuss their possible functional implications.

scholarly journals The mutationnrpb1-A325Vin the largest subunit of RNA polymerase II suppresses compromised growth ofArabidopsisplants deficient in a function of the general transcription factor IIF

2017 ◽  
Vol 89 (4) ◽  
pp. 730-745 ◽  
Author(s):  
Elena Babiychuk ◽  
Khai Trinh Hoang ◽  
Klaas Vandepoele ◽  
Eveline Van De Slijke ◽  
Danny Geelen ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
General Transcription Factor ◽  
Transcription Factor Iif

The general transcription factor RAP30 binds to RNA polymerase II and prevents it from binding nonspecifically to DNA

1992 ◽  
Vol 12 (1) ◽  
pp. 30-37
Author(s):  
M T Killeen ◽  
J F Greenblatt
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Small Subunit ◽  
Glutathione S Transferase ◽  
General Transcription Factor ◽  
Indirect Consequence ◽  
Transcription In Vitro ◽  
Sigma 70

RAP30/74 is a human general transcription factor that binds to RNA polymerase II and is required for initiation of transcription in vitro regardless of whether the promoter has a recognizable TATA box (Z. F. Burton, M. Killeen, M. Sopta, L. G. Ortolan, and J. F. Greenblatt, Mol. Cell. Biol. 8:1602-1613, 1988). Part of the amino acid sequence of RAP30, the small subunit of RAP30/74, has limited homology with part of Escherichia coli sigma 70 (M. Sopta, Z. F. Burton, and J. Greenblatt, Nature (London) 341:410-414, 1989). To determine which sigmalike activities of RAP30/74 could be attributed to RAP30, we purified human RAP30 and a RAP30-glutathione-S-transferase fusion protein that had been produced in E. coli. Bacterially produced RAP30 bound to RNA polymerase II in the absence of RAP74. Both partially purified natural RAP30/74 and recombinant RAP30 prevented RNA polymerase II from binding nonspecifically to DNA. In addition, nonspecific transcription by RNA polymerase II was greatly inhibited by RAP30-glutathione-S-transferase. DNA-bound RNA polymerase II could be removed from DNA by partially purified RAP30/74 but not by bacterially expressed RAP30. Thus, the ability of RAP30/74 to recruit RNA polymerase II to a promoter-bound preinitiation complex may be an indirect consequence of its ability to suppress nonspecific binding of RNA polymerase II to DNA.

scholarly journals Mutations in the second-largest subunit of Drosophila RNA polymerase II interact with Ubx.

Genetics ◽  
1992 ◽  
Vol 131 (4) ◽  
pp. 895-903
Author(s):  
M A Mortin ◽  
R Zuerner ◽  
S Berger ◽  
B J Hamilton
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Thoracic Segment ◽  
Mutant Phenotype ◽  
Analogous Structure ◽  
Gene Encoding ◽  
Recessive Lethal ◽  
The Third ◽  
Complementation Groups

Abstract Specific mutations in the gene encoding the largest subunit of RNA polymerase II (RpII215) cause a partial transformation of a structure of the third thoracic segment, the capitellum, into the analogous structure of the second thoracic segment, the wing. This mutant phenotype is also caused by genetically reducing the cellular concentration of the transcription factor Ultrabithorax (Ubx). To recover mutations in the 140,000-D second-largest subunit of RNA polymerase II (RpII140) and determine whether any can cause a mutant phenotype similar to Ubx we attempted to identify all recessive-lethal mutable loci in a 340-kilobase deletion including this and other loci. One of the 13 complementation groups in this region encodes RpII140. Three RpII140 alleles cause a transformation of capitellum to wing but unlike RpII215 alleles, only when the concentration of Ubx protein is reduced by mutations in Ubx.

scholarly journals A heteromeric transcription factor required for mammalian RNA polymerase II

1990 ◽  
Vol 18 (16) ◽  
pp. 4843-4849 ◽  
Author(s):  
Shigetaka Kitajima ◽  
Yujiro Tanaka ◽  
Tatsuo Kawaguchi ◽  
Takayuki Nagaoka ◽  
Sherman M. Weissman ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Rna Polymerase Ii
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