IDENTIFICATION OF A RECOMBINATIONAL SIGNAL SEQUENCE-SPECIFIC DNA-BINDING PROTEIN(S) OF Mr115,000 IN THE NUCLEAR EXTRACTS FROM IMMATURE LYMPHOID CELL LINES

1990 ◽  
Vol 17 (1-2) ◽  
pp. 67-75 ◽  
Author(s):  
S. Miyake ◽  
H. Sugiyama ◽  
Y. Tani ◽  
T. Fukuda ◽  
S. Kishimoto
2010 ◽  
Vol 222 (03) ◽  
Author(s):  
S Degen ◽  
S Kuhfittig-Kulle ◽  
JH Schulte ◽  
F Westermann ◽  
A Schramm ◽  
...  

1989 ◽  
Vol 9 (3) ◽  
pp. 1351-1356 ◽  
Author(s):  
D L Zhang ◽  
K C Ehrlich ◽  
P C Supakar ◽  
M Ehrlich

A novel, 5-methylcytosine-specific, DNA-binding protein, DBP-m, has been identified in nuclear extracts of peas. DBP-m specifically recognizes 5-methylcytosine residues in DNA without appreciable DNA sequence specificity, unlike a mammalian DNA-binding protein (MDBP), which recognizes 5-methylcytosine residues but only in a related family of 14-base-pair sequences.


2013 ◽  
Vol 94 (6) ◽  
pp. 1325-1334 ◽  
Author(s):  
Yadvinder S. Ahi ◽  
Sai V. Vemula ◽  
Suresh K. Mittal

Adenovirus (AdV) is thought to follow a sequential assembly pathway similar to that observed in dsDNA bacteriophages and herpesviruses. First, empty capsids are assembled, and then the genome is packaged through a ring-like structure, referred to as a portal, located at a unique vertex. In human AdV serotype 5 (HAdV5), the IVa2 protein initiates specific recognition of viral genome by associating with the viral packaging domain located between nucleotides 220 and 400 of the genome. IVa2 is located at a unique vertex on mature capsids and plays an essential role during genome packaging, most likely by acting as a DNA packaging ATPase. In this study, we demonstrated interactions among IVa2, 33K and DNA-binding protein (DBP) in virus-infected cells by in vivo cross-linking of HAdV5-infected cells followed by Western blot, and co-immunoprecipitation of IVa2, 33K and DBP from nuclear extracts of HAdV5-infected cells. Confocal microscopy demonstrated co-localization of IVa2, 33K and DBP in virus-infected cells and also in cells transfected with IVa2, 33K and DBP genes. Immunogold electron microscopy of purified HAdV5 showed the presence of IVa2, 33K or DBP at a single site on the virus particles. Our results provide indirect evidence that IVa2, 33K and DBP may form a complex at a unique vertex on viral capsids and cooperate in genome packaging.


1992 ◽  
Vol 112 (3) ◽  
pp. 314-320 ◽  
Author(s):  
Yasushi Hamaguchi ◽  
Yoshiki Yamamoto ◽  
Hiroko Iwanari ◽  
Shingo Maruyama ◽  
Takahisa Furukawa ◽  
...  

1993 ◽  
Vol 156 (2) ◽  
pp. 409-417 ◽  
Author(s):  
Judith Litvin ◽  
Michael O. Montgomery ◽  
David J. Goldhamer ◽  
Charles P. Emerson ◽  
David M. Bader

FEBS Letters ◽  
1992 ◽  
Vol 298 (2-3) ◽  
pp. 240-244 ◽  
Author(s):  
Takaaki Iwasaki ◽  
Yoshimasa Uehara ◽  
Lee Graves ◽  
Nisa Rachie ◽  
Karol Bomsztyk

Virology ◽  
1992 ◽  
Vol 190 (2) ◽  
pp. 624-634 ◽  
Author(s):  
Douglas E. Brough ◽  
Vaughn Cleghon ◽  
Daniel F. Klessig

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