scholarly journals Biophysical Characterization of the DNA Binding Domain of gpNu1, a Viral DNA Packaging Protein

2001 ◽  
Vol 276 (23) ◽  
pp. 20175-20181 ◽  
Author(s):  
David L. Bain ◽  
Nancy Berton ◽  
Marcos Ortega ◽  
Jennifer Baran ◽  
Qin Yang ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dna Packaging ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Viral Dna ◽  
Biophysical Characterization ◽  
Viral Dna Packaging

Domain Substructure of HPV E6 Oncoprotein:  Biophysical Characterization of the E6 C-Terminal DNA-Binding Domain†

Biochemistry ◽  
2003 ◽  
Vol 42 (17) ◽  
pp. 4909-4917 ◽  
Author(s):  
Yves Nominé ◽  
Sebastian Charbonnier ◽  
Tutik Ristriani ◽  
Gunter Stier ◽  
Murielle Masson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Biophysical Characterization ◽  
Hpv E6 ◽  
E6 Oncoprotein

Cloning, Expression, and Characterization of a DNA Binding Domain of gpNu1, a Phage λ DNA Packaging Protein†

Biochemistry ◽  
1999 ◽  
Vol 38 (1) ◽  
pp. 465-477 ◽  
Author(s):  
Qin Yang ◽  
Tonny de Beer ◽  
Liping Woods ◽  
Jeffrey D. Meyer ◽  
Mark C. Manning ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dna Packaging ◽  
Binding Domain ◽  
Dna Binding Domain

Biophysical characterization of the c-myb DNA-binding domain

Biochemistry ◽  
1994 ◽  
Vol 33 (48) ◽  
pp. 14586-14593 ◽  
Author(s):  
Andreas Ebneth ◽  
Olaf Schweers ◽  
Hubert Thole ◽  
Ursula Fagin ◽  
Claus Urbanke ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Biophysical Characterization

scholarly journals Characterization of the Elk-1 ETS DNA-binding Domain

1995 ◽  
Vol 270 (11) ◽  
pp. 5805-5811 ◽  
Author(s):  
Paul Shore ◽  
Louise Bisset ◽  
Jeremy Lakey ◽  
Jonathan P. Waltho ◽  
Richard Virden ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain

Characterization of Spi-B, a transcription factor related to the putative oncoprotein Spi-1/PU.1

1992 ◽  
Vol 12 (10) ◽  
pp. 4297-4304 ◽  
Author(s):  
D Ray ◽  
R Bosselut ◽  
J Ghysdael ◽  
M G Mattei ◽  
A Tavitian ◽  
...  
Keyword(s):  
Dna Binding ◽  
Cell Lines ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
New Gene ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hematopoietic Cell Lines

We have cloned a human cDNA from a new gene, spi-B, on the basis of its homology with the DNA-binding domain of the Spi-1/PU.1 putative oncogene product. spi-B codes for a protein of 262 amino acids presenting 43% overall identity with Spi-1. Its highly basic carboxy-terminal region exhibits 34% sequence identity with the DNA-binding domain of the Ets-1 protein. We showed that the Spi-B protein is able to bind the purine-rich sequence (PU box) recognized by Spi-1/PU.1 and to activate transcription of a reporter plasmid containing PU boxes. Chromosome in situ hybridization allowed us to map spi-B to the 19q13.3-19q13.4 region of the human genome. spi-B, like spi-1, was found to be expressed in various murine and human hematopoietic cell lines except T lymphoid cell lines.

Production and characterization of a retinoic acid receptor RARγ construction encompassing the DNA binding domain and the disordered N-terminal proline rich domain

2014 ◽  
Vol 95 ◽  
pp. 113-120 ◽  
Author(s):  
Denise Martinez-Zapien ◽  
Marc-André Delsuc ◽  
Gilles Travé ◽  
Régis Lutzing ◽  
Cécile Rochette-Egly ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Acid Receptor ◽  
Rich Domain

scholarly journals Herpes Simplex Virus Type 1 C-Terminal Variants of the Origin Binding Protein (OBP), OBPC-1 and OBPC-2, Cooperatively Regulate Viral DNA Levels In Vitro, and OBPC-2 Affects Mortality in Mice

2007 ◽  
Vol 81 (19) ◽  
pp. 10699-10711 ◽  
Author(s):  
Malen A. Link ◽  
Priscilla A. Schaffer
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Viral Dna ◽  
Viral Dna Replication ◽  
Origin Binding Protein ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Two in-frame, C-terminal isoforms of the herpes simplex virus type 1 (HSV-1) origin binding protein (OBP), OBPC-1 and OBPC-2, and a unique C-terminal transcript, UL8.5, are specified by HSV-1 DNA. As the first isoform identified, OBPC-1 was initially assumed to be the product of the UL8.5 transcript. Recent evidence has demonstrated, however, that OBPC-1 is a cathepsin B-mediated cleavage product of OBP, suggesting that OBPC-2 is the product of the UL8.5 transcript. Because both OBPC-1 and -2 contain the majority of the OBP DNA binding domain, we hypothesized that both may be involved in regulating origin-dependent, OBP-mediated viral DNA replication. In this paper, we demonstrate that OBPC-2 is, indeed, the product of the UL8.5 transcript. The translational start site of OBPC-2 was mapped, and a virus (M571A) that does not express this protein efficiently was constructed. Using M571A, we have shown that OBPC-2 is able to bind origin DNA, even though it lacks seven N-terminal amino acid residues of the previously mapped OBP DNA binding domain, resulting in a revision of the limits of the OBP DNA binding domain. Consistent with their proposed roles in regulating viral DNA replication, OBPC-1 and -2 act together to down-regulate viral DNA replication in vitro. During functional studies in vivo, OBPC-2 was identified as a factor that increases mortality in the mouse ocular model of HSV-1 infection.

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