scholarly journals xUBF, an RNA polymerase I transcription factor, binds crossover DNA with low sequence specificity.

1994 ◽  
Vol 14 (5) ◽  
pp. 2871-2882 ◽  
Author(s):  
C H Hu ◽  
B McStay ◽  
S W Jeong ◽  
R H Reeder
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Intact Protein ◽  
Sequence Specificity ◽  
Binding Motifs ◽  
Double Helices ◽  
Dna Binding Motifs ◽  
Polymerase I

Xenopus UBF (xUBF) is a transcription factor for RNA polymerase I which contains multiple DNA-binding motifs. These include a short basic region adjacent to a dimer motif plus five high-mobility-group (HMG) boxes. All of these DNA-binding motifs exhibit low sequence specificity, whether assayed singly or together. In contrast, the HMG boxes recognize DNA structure that is formed when two double helices are crossed over each other. HMG box 1, in particular, requires association of two double helices before it will bind and, either by itself or in the context of the intact protein, will loop DNA and organize it into higher-order structures. We discuss how this mode of binding affects the function of xUBF as a transcription factor.

rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs

1990 ◽  
Vol 10 (7) ◽  
pp. 3810-3812
Author(s):  
C S Pikaard ◽  
S D Smith ◽  
R H Reeder ◽  
L Rothblum
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Affinity Purification ◽  
Binding Specificity ◽  
Rna Polymerase I ◽  
Dna Binding Specificity ◽  
Apparent Homogeneity ◽  
And Function ◽  
Polymerase I

Rat cells contain a DNA-binding polymerase I transcription factor, rUBF, with properties similar to UBF homologs that have been purified from both human (hUBF) and frog (xUBF) cells. In this note we report the affinity purification of rUBF to apparent homogeneity and show that UBFs from both rat and frog have identical footprinting characteristics on templates from either species. Furthermore, xUBF was able to stimulate transcription from rat RNA polymerase I promoters in a partially fractionated rat extract that was UBF dependent. These results strengthen the conclusion that all vertebrate cells contain a UBF homolog whose DNA-binding specificity and function have been strongly conserved.

scholarly journals rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs.

1990 ◽  
Vol 10 (7) ◽  
pp. 3810-3812 ◽  
Author(s):  
C S Pikaard ◽  
S D Smith ◽  
R H Reeder ◽  
L Rothblum
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Affinity Purification ◽  
Binding Specificity ◽  
Rna Polymerase I ◽  
Dna Binding Specificity ◽  
Apparent Homogeneity ◽  
And Function ◽  
Polymerase I

Rat cells contain a DNA-binding polymerase I transcription factor, rUBF, with properties similar to UBF homologs that have been purified from both human (hUBF) and frog (xUBF) cells. In this note we report the affinity purification of rUBF to apparent homogeneity and show that UBFs from both rat and frog have identical footprinting characteristics on templates from either species. Furthermore, xUBF was able to stimulate transcription from rat RNA polymerase I promoters in a partially fractionated rat extract that was UBF dependent. These results strengthen the conclusion that all vertebrate cells contain a UBF homolog whose DNA-binding specificity and function have been strongly conserved.

scholarly journals Analysis of the phosphorylation, DNA-binding and dimerization properties of the RNA polymerase I transcription factors UBF1 and UBF2

1992 ◽  
Vol 20 (6) ◽  
pp. 1301-1308 ◽  
Author(s):  
Daniel J.O. Mahony ◽  
S. David Smith ◽  
WenQin Xie ◽  
Lawrence I. Rothblum
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Polymerase I

Immunization of nonautoimmune mice with DNA binding domains of the largest subunit of RNA polymerase I results in production of anti-dsDNA and anti-Sm/RNP antibodies

Autoimmunity ◽  
2007 ◽  
Vol 40 (1) ◽  
pp. 38-47 ◽  
Author(s):  
Sandra A. Sciascia ◽  
Sandra A. Sciascia ◽  
Kristina Robson ◽  
Sandra A. Sciascia ◽  
Kristina Robson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase I ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Polymerase I

scholarly journals Characterization of a Novel Class I Transcription Factor A (CITFA) Subunit That Is Indispensable for Transcription by the Multifunctional RNA Polymerase I of Trypanosoma brucei

2012 ◽  
Vol 11 (12) ◽  
pp. 1573-1581 ◽  
Author(s):  
Tu N. Nguyen ◽  
Bao N. Nguyen ◽  
Ju Huck Lee ◽  
Aswini K. Panigrahi ◽  
Arthur Günzl
Keyword(s):  
Transcription Factor ◽  
Rna Polymerase ◽  
Trypanosoma Brucei ◽  
Rna Polymerase I ◽  
Class I ◽  
Mammalian Host ◽  
Subunit Structure ◽  
Content Type ◽  
Pol I ◽  
Polymerase I

ABSTRACT Trypanosoma brucei is the only organism known to have evolved a multifunctional RNA polymerase I (pol I) system that is used to express the parasite's ribosomal RNAs, as well as its major cell surface antigens, namely, the variant surface glycoprotein (VSG) and procyclin, which are vital for establishing successful infections in the mammalian host and the tsetse vector, respectively. Thus far, biochemical analyses of the T. brucei RNA pol I transcription machinery have elucidated the subunit structure of the enzyme and identified the class I transcription factor A (CITFA). CITFA binds to RNA pol I promoters, and its CITFA-2 subunit was shown to be absolutely essential for RNA pol I transcription in the parasite. Tandem affinity purification (TAP) of CITFA revealed the subunits CITFA-1 to -6, which are conserved only among kinetoplastid organisms, plus the dynein light chain DYNLL1. Here, by tagging CITFA-6 instead of CITFA-2, a complex was purified that contained all known CITFA subunits, as well as a novel proline-rich protein. Functional studies carried out in vivo and in vitro , as well as a colocalization study, unequivocally demonstrated that this protein is a bona fide CITFA subunit, essential for parasite viability and indispensable for RNA pol I transcription of ribosomal gene units and the active VSG expression site in the mammalian-infective life cycle stage of the parasite. Interestingly, CITFA-7 function appears to be species specific, because expression of an RNA interference (RNAi)-resistant CITFA-7 transgene from Trypanosoma cruzi could not rescue the lethal phenotype of silencing endogenous CITFA-7 .

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