Induction of paranodal myelin detachment and sodium channel loss in vivo by Campylobacter jejuni DNA-binding protein from starved cells (C-Dps) in myelinated nerve fibers

2010 ◽  
Vol 288 (1-2) ◽  
pp. 54-62 ◽  
Author(s):  
Hua Piao ◽  
Motozumi Minohara ◽  
Nobutoshi Kawamura ◽  
Wei Li ◽  
Yoshimitsu Mizunoe ◽  
...  
Keyword(s):  
Dna Binding ◽  
Sodium Channel ◽  
Campylobacter Jejuni ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Nerve Fibers ◽  
Myelinated Nerve ◽  
Myelinated Nerve Fibers ◽  
Channel Loss

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

The DNA Binding Protein H-NS Binds to and Alters the Stability of RNA in vitro and in vivo

2004 ◽  
Vol 339 (3) ◽  
pp. 505-514 ◽  
Author(s):  
Cristin C Brescia ◽  
Meenakshi K Kaw ◽  
Darren D Sledjeski
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
The Stability

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.

scholarly journals High Affinity binding of Yeast Nucleolin Nsr1 to Co-transcriptionally Formed G4 DNA Obstructs Replication and Elevates Genome Instability

2019 ◽  
Author(s):  
Shivani Singh ◽  
Alexandra Berroyer ◽  
Minseon Kim ◽  
Nayun Kim
Keyword(s):  
Dna Binding ◽  
Genome Instability ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Yeast Genome ◽  
Stable Complex ◽  
High Affinity ◽  
G4 Dna ◽  
G Quadruplex

ABSTRACTA significant increase in genome instability is associated with the conformational shift of a guanine-run-containing DNA strand into the four-stranded G-quadruplex (G4) DNA. The mechanism underlying the recombination and genome rearrangements following the formation of G4 DNA in vivo has been difficult to elucidate but has become better clarified by the identification and functional characterization of several key G4 DNA-binding proteins. Mammalian nucleolin NCL is a highly specific G4 DNA-binding protein with a well-defined role in the transcriptional regulation of genes with associated G4 DNA-forming sequence motifs at their promoters. The consequence of the in vivo interaction between G4 DNA and nucleolin in respect to the genome instability has not been previously investigated. We show here that G4 DNA-binding is a conserved function in the yeast nucleolin Nsr1. Furthermore, we demonstrate that the Nsr1-G4 DNA complex formation results in replication obstruction and is a major factor in inducing the genome instability associated with the co-transcriptionally formed G4 DNA in the yeast genome. The G4-associated genome instability and the G4 DNA-binding in vivo requires the arginine-glycine-glycine (RGG) repeats located at the C-terminus of the Nsr1 protein. Nsr1 with the deletion of RGG domain supports normal cell growth and is sufficient for its pre-rRNA processing function. However, the truncation of RGG domain of Nsr1 significantly weakens its interaction with G4 DNA in vitro and in vivo and restores unhindered replication, overall resulting in a sharp reduction in the G4-associated genome instability. Our data suggest that the interaction between Nsr1 with the intact RGG repeats and G4 DNA impairs genome stability by precluding the access of G4-resolving proteins and obstructing replication.AUTHOR SUMMARYGenome instability is uniquely elevated at sequences containing multiple runs of guanines, which can fold into the unusual, four-stranded G-quadruplex (G4) DNA. In this study, we report a novel finding that a highly conserved G4 DNA binding protein Nsr1 can elevate the rate of recombination and chromosomal rearrangement occurring at a G4 DNA-forming sequence in the genome of Saccharomyces cerevisiae. The elevated genome instability requires the C-terminally located RGG domain of Nsr1, which supports the high-affinity interaction between the protein and G4 DNA. The connection between G4-specific genome instability and the function of Nsr1 to form stable complex with G4 DNA led to the hypothesis that the high-affinity Nsr1-G4 DNA complexes can become a barrier to replication. We demonstrate here that the presence of Nsr1 in fact slows the replication past a G4 DNA-containing genomic site and that the RGG domain is required to facilitate such replication block.

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