scholarly journals The DNA-binding properties of a rat nuclear phosphoprotein

1991 ◽  
Vol 274 (3) ◽  
pp. 687-691 ◽  
Author(s):  
D B Cowan ◽  
G Chaban ◽  
C C Liew
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Nuclear Antigen ◽  
Binding Properties ◽  
Nucleosomal Dna ◽  
Dna Binding Site ◽  
Nuclear Phosphoprotein ◽  
Dna Binding Properties ◽  
Synthetic Oligonucleotides ◽  
Competition Assays

The non-histone nuclear phosphoprotein B2 (Mr 68,000; pI 6.5-8.2) was found to bind specifically defined fragments of DNA. With the use of monoclonal IgG2A antibodies prepared against this nuclear antigen, nucleosomal DNA fragments associated with phosphoprotein B2 were isolated and cloned. Nine cloned fragments were sequenced and analysed for similarity. The clone having the most similarity to the others was chosen to serve as a model in gel shift and footprinting assays. Subsequently, the DNA binding site was found to reside within a 30 bp region. Synthetic oligonucleotides corresponding to this site confirmed the specificity of DNA binding exhibited by the nuclear antigen as demonstrated in competition assays. Moreover, a 5′-TATTAG/C-3′ motif was found to exist within the binding site and in the other sequenced clones, possibly implicating the involvement of this motif in protein binding.

scholarly journals A yeast protein possesses the DNA-binding properties of the adenovirus major late transcription factor.

1989 ◽  
Vol 9 (2) ◽  
pp. 820-822 ◽  
Author(s):  
L A Chodosh ◽  
S Buratowski ◽  
P A Sharp
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Site ◽  
Upstream Stimulatory Factor ◽  
Binding Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Human Promoter ◽  
Late Transcription ◽  
Stimulatory Factor ◽  
Dna Binding Properties

The adenovirus major late transcription factor (MLTF), or upstream stimulatory factor, is a human promoter-specific transcription factor which recognizes the near-palindromic sequence GGCCACGTGACC (R. W. Carthew, L. A. Chodosh, and P. A. Sharp, Cell 43:439-448, 1985; L. A. Chodosh, R. W. Carthew, and P. A. Sharp, Mol. Cell. Biol. 6:4723-4733, 1986; M. Sawadogo and R. G. Roeder, Cell 43:165-175, 1985). We describe here a protein found in the yeast Saccharomyces cerevisiae which possesses DNA-binding properties that are virtually identical to those of human MLTF. These two proteins recognize the same DNA-binding site, make the same purine nucleotide contacts, and are affected in the same manner by mutations in the MLTF-binding site.

DNA-binding properties of nuclear matrix proteins

1978 ◽  
Vol 34 (1) ◽  
pp. 233-246 ◽  
Author(s):  
D.E. Comings ◽  
A.S. Wallack
Keyword(s):  
Dna Binding ◽  
Nuclear Matrix ◽  
Matrix Proteins ◽  
Binding Properties ◽  
E Coli ◽  
Nuclear Matrix Proteins ◽  
The Matrix ◽  
Filter Assay ◽  
Dna Binding Properties ◽  
Competition Assays

Mouse nuclear matrix proteins, examined by a filter assay, were found to bind to DNA. There was no preference for homologous mouse compared to heterologous E. coli DNA. Competition assays showed a preference for AT-rich DNA and of the 4 single-stranded homopolymers there was a preference for poly(dT). These observations are consistent with the possibility that the matrix may play a role in the formation of AT-rich chromomeres (G-bands).

scholarly journals Myeloperoxidase: a myeloid cell nuclear antigen with DNA-binding properties.

1988 ◽  
Vol 85 (4) ◽  
pp. 1232-1236 ◽  
Author(s):  
S. Murao ◽  
F. J. Stevens ◽  
A. Ito ◽  
E. Huberman
Keyword(s):  
Dna Binding ◽  
Myeloid Cell ◽  
Nuclear Antigen ◽  
Binding Properties ◽  
Dna Binding Properties

A yeast protein possesses the DNA-binding properties of the adenovirus major late transcription factor

1989 ◽  
Vol 9 (2) ◽  
pp. 820-822
Author(s):  
L A Chodosh ◽  
S Buratowski ◽  
P A Sharp
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Site ◽  
Upstream Stimulatory Factor ◽  
Binding Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Human Promoter ◽  
Late Transcription ◽  
Stimulatory Factor ◽  
Dna Binding Properties

The adenovirus major late transcription factor (MLTF), or upstream stimulatory factor, is a human promoter-specific transcription factor which recognizes the near-palindromic sequence GGCCACGTGACC (R. W. Carthew, L. A. Chodosh, and P. A. Sharp, Cell 43:439-448, 1985; L. A. Chodosh, R. W. Carthew, and P. A. Sharp, Mol. Cell. Biol. 6:4723-4733, 1986; M. Sawadogo and R. G. Roeder, Cell 43:165-175, 1985). We describe here a protein found in the yeast Saccharomyces cerevisiae which possesses DNA-binding properties that are virtually identical to those of human MLTF. These two proteins recognize the same DNA-binding site, make the same purine nucleotide contacts, and are affected in the same manner by mutations in the MLTF-binding site.

scholarly journals Differential DNA Binding of Transcriptional Regulator PcaU from Acinetobacter sp. Strain ADP1

2002 ◽  
Vol 184 (7) ◽  
pp. 1988-1997 ◽  
Author(s):  
Roland Popp ◽  
Tobias Kohl ◽  
Patricia Patz ◽  
Gaby Trautwein ◽  
Ulrike Gerischer
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Binding Sites ◽  
Specific Binding ◽  
Transcriptional Regulator ◽  
Intrinsic Curvature ◽  
Binding Properties ◽  
Expression Of Genes ◽  
Intergenic Dna ◽  
Dna Binding Properties

ABSTRACT Transcriptional regulator PcaU from Acinetobacter sp. strain ADP1 governs expression of genes for protocatechuate degradation (pca genes) as a repressor or an activator depending on the levels of the inducer protocatechuate and of its own gene. PcaU is a member of the IclR protein family. Here the DNA binding properties of the purified protein are described in terms of the location of the binding sites and the affinity to these sites. Native PcaU was purified after overexpression of the pcaU gene in Escherichia coli. It is a dimer in solution. The binding site in the pcaU-pcaI intergenic region is located between the two divergent promoters covering 45 bp, which includes three perfect 10-bp repetitions. A PcaU binding site downstream of pcaU is covered by PcaU across two palindromic sequence repetitions. The affinity of PcaU for the intergenic binding sites is 50-fold higher (dissociation constant [Kd ], 0.16 nM) than the affinity for the site downstream of pcaU (Kd , 8 nM). The binding of PcaU was tested after modifications of the intergenic binding site. Removal of any external sequence repetition still allowed for specific binding of PcaU, but the affinity was significantly reduced, suggesting an important role for all three sequence repetitions in gene expression. The involvement of DNA bending in the regulatory process is suggested by the observed strong intrinsic curvature displayed by the pcaU-pcaI intergenic DNA.

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