Computer-assisted primary and secondary structure analyses of DNA polymerases of herpes simplex, Epstein-Barr and varicella zoster viruses reveal conserved domains with some homology to DNA-binding domain in E. coli DNA pol I

Virus Genes ◽  
1988 ◽  
Vol 1 (4) ◽  
Author(s):  
Yechiel Becker
Keyword(s):  
Herpes Simplex ◽  
Secondary Structure ◽  
Dna Binding ◽  
Dna Polymerases ◽  
Computer Assisted ◽  
Dna Binding Domain ◽  
Varicella Zoster ◽  
E Coli ◽  
Pol I ◽  
Epstein Barr

scholarly journals Water Release upon DNA Binding by E. coli and T. aquaticus Pol I DNA Polymerases

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
John T. Baker ◽  
Daniel J. Deredge ◽  
Kausiki Datta ◽  
Vince J. LiCata
Keyword(s):  
Dna Binding ◽  
Dna Polymerases ◽  
Water Release ◽  
E Coli ◽  
Pol I

scholarly journals DNA Binding Activity of the Herpes Simplex Virus Type 1 Origin Binding Protein, UL9, Can Be Modulated by Sequences in the N Terminus: Correlation between Transdominance and DNA Binding

2006 ◽  
Vol 80 (9) ◽  
pp. 4491-4500 ◽  
Author(s):  
Soma Chattopadhyay ◽  
Sandra K. Weller
Keyword(s):  
Herpes Simplex ◽  
Dna Binding ◽  
Binding Activity ◽  
Plaque Formation ◽  
Dna Binding Domain ◽  
Dna Binding Activity ◽  
Origin Binding Protein ◽  
N Terminus ◽  
Simplex Virus

ABSTRACT UL9, the origin binding protein of herpes simplex virus type 1, is a member of the SF2 family of helicases. Cotransfection of cells with infectious viral DNA and plasmids expressing either full-length UL9 or the C-terminal DNA binding domain alone results in the drastic inhibition of plaque formation which can be partially relieved by an insertion mutant lacking DNA binding activity. In this work, C-terminally truncated mutants which terminate at or near residue 359 were shown to potentiate plaque formation, while other C-terminal truncations were inhibitory. Thus, residues in the N-terminal region appear to regulate the inhibitory properties of UL9. To identify which residues were involved in this regulation, a series of N-terminally truncated mutants were constructed which contain the DNA binding domain and various N-terminal extensions. Mutants whose N terminus is either at residue 494 or 535 were able to bind the origin efficiently and were inhibitory to plaque formation, whereas constructs whose N terminus is at residue 304 or 394 were defective in origin binding activity and were able to relieve inhibition. Since UL9 is required for viral infection at early but not late times and is inhibitory to infection when overexpressed, we propose that the DNA binding activities of UL9 are regulated during infection. For infection to proceed, UL9 may need to switch from a DNA binding to a non-DNA binding mode, and we suggest that sequences residing in the N terminus play a role in this switch.

scholarly journals Secondary structure and folding topology of the DNA binding domain of interferon regulatory factor 2, as revealed by NMR spectroscopy

FEBS Letters ◽  
1995 ◽  
Vol 359 (2-3) ◽  
pp. 184-188 ◽  
Author(s):  
Koichi Uegaki ◽  
Masahiro Shirakawa ◽  
Hisashi Harada ◽  
Tadatsugu Taniguchi ◽  
Yoshimasa Kyogoku
Keyword(s):  
Nmr Spectroscopy ◽  
Secondary Structure ◽  
Dna Binding ◽  
Interferon Regulatory Factor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Regulatory Factor

The DNA binding domain and bending angle of E. coli CAP protein

Cell ◽  
1986 ◽  
Vol 47 (6) ◽  
pp. 995-1005 ◽  
Author(s):  
Huei-Nin Liu-Johnson ◽  
Marc R. Gartenberg ◽  
Donald M. Crothers
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Bending Angle ◽  
E Coli

NMR studies of the POU-specific DNA-binding domain of Oct-1: Sequential proton and nitrogen-15 assignments and secondary structure

Biochemistry ◽  
1993 ◽  
Vol 32 (23) ◽  
pp. 6032-6040 ◽  
Author(s):  
Michel Cox ◽  
Niek Dekker ◽  
Rolf Boelens ◽  
C. Peter Verrijzer ◽  
Peter C. van der Vliet ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies
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