scholarly journals Adenoviral E2 IVa2 protein interacts with L4 33K protein and E2 DNA-binding protein

2013 ◽  
Vol 94 (6) ◽  
pp. 1325-1334 ◽  
Author(s):  
Yadvinder S. Ahi ◽  
Sai V. Vemula ◽  
Suresh K. Mittal
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Indirect Evidence ◽  
Dna Binding Protein ◽  
Immunogold Electron Microscopy ◽  
Genome Packaging ◽  
Nuclear Extracts ◽  
Infected Cells ◽  
Unique Vertex

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.

Adenovirus type 2 coded single-stranded DNA binding protein: in vivo phosphorylation and modification.

1977 ◽  
Vol 22 (2) ◽  
pp. 402-411 ◽  
Author(s):  
Y H Jeng ◽  
W S Wold ◽  
K Sugawara ◽  
Z Gilead ◽  
M Green
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Adenovirus Type ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Adenovirus Type 2

scholarly journals A plant DNA-binding protein that recognizes 5-methylcytosine residues.

1989 ◽  
Vol 9 (3) ◽  
pp. 1351-1356 ◽  
Author(s):  
D L Zhang ◽  
K C Ehrlich ◽  
P C Supakar ◽  
M Ehrlich
Keyword(s):  
Dna Binding ◽  
Dna Sequence ◽  
Base Pair ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Sequence Specificity ◽  
Dna Sequence Specificity ◽  
Plant Dna ◽  
Related Family ◽  
Nuclear Extracts

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.

scholarly journals The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Antoine Hocher ◽  
Maria Rojec ◽  
Jacob B Swadling ◽  
Alexander Esin ◽  
Tobias Warnecke
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Coli Strain ◽  
Micrococcal Nuclease ◽  
Thermoplasma Acidophilum ◽  
Chromatin Architecture ◽  
Archaeal Histone

Histones are a principal constituent of chromatin in eukaryotes and fundamental to our understanding of eukaryotic gene regulation. In archaea, histones are widespread but not universal: several lineages have lost histone genes. What prompted or facilitated these losses and how archaea without histones organize their chromatin remains largely unknown. Here, we elucidate primary chromatin architecture in an archaeon without histones, Thermoplasma acidophilum, which harbors a HU family protein (HTa) that protects part of the genome from micrococcal nuclease digestion. Charting HTa-based chromatin architecture in vitro, in vivo and in an HTa-expressing E. coli strain, we present evidence that HTa is an archaeal histone analog. HTa preferentially binds to GC-rich sequences, exhibits invariant positioning throughout the growth cycle, and shows archaeal histone-like oligomerization behavior. Our results suggest that HTa, a DNA-binding protein of bacterial origin, has converged onto an architectural role filled by histones in other archaea.

LaTBP1: A Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domain

2007 ◽  
Vol 465 (2) ◽  
pp. 399-409 ◽  
Author(s):  
Cristina B.B. Lira ◽  
Jair L. de Siqueira Neto ◽  
Letícia Khater ◽  
Thiago C. Cagliari ◽  
Luis A. Peroni ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Leishmania Amazonensis

scholarly journals Enteroviral Infection Leads to Transactive Response DNA-Binding Protein 43 Pathology in Vivo

2018 ◽  
Vol 188 (12) ◽  
pp. 2853-2862 ◽  
Author(s):  
Yuan Chao Xue ◽  
Chelsea M. Ruller ◽  
Gabriel Fung ◽  
Yasir Mohamud ◽  
Haoyu Deng ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Enteroviral Infection

scholarly journals Remodeling a DNA-binding protein as a specific in vivo inhibitor of bacterial secretin PulD

2007 ◽  
Vol 104 (46) ◽  
pp. 17983-17988 ◽  
Author(s):  
B. Mouratou ◽  
F. Schaeffer ◽  
I. Guilvout ◽  
D. Tello-Manigne ◽  
A. P. Pugsley ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein

Cytomegalovirus-infected cells contain a DNA-binding protein

Virology ◽  
1981 ◽  
Vol 111 (1) ◽  
pp. 251-262 ◽  
Author(s):  
Wade Gibson ◽  
Theresa L. Murphy ◽  
Clinton Roby
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Infected Cells
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