scholarly journals Structural Dynamics and Single-Stranded DNA Binding Activity of the Three N-Terminal Domains of the Large Subunit of Replication Protein A from Small Angle X-ray Scattering

Biochemistry ◽  
2010 ◽  
Vol 49 (13) ◽  
pp. 2880-2889 ◽  
Author(s):  
Dalyir I. Pretto ◽  
Susan Tsutakawa ◽  
Chris A. Brosey ◽  
Amalchi Castillo ◽  
Marie-Eve Chagot ◽  
...  
Keyword(s):  
Dna Binding ◽  
Structural Dynamics ◽  
Small Angle ◽  
Large Subunit ◽  
Protein A ◽  
Replication Protein A ◽  
Binding Activity ◽  
X Ray ◽  
Dna Binding Activity ◽  
X Ray Scattering

scholarly journals Sequence-specific DNA binding activity in the RAE28 protein, a mouse homologue of the Drosophila polyhomeotic protein

IUBMB Life ◽  
1998 ◽  
Vol 46 (5) ◽  
pp. 905-912
Author(s):  
Midori Nomura ◽  
Yoshihiro Takihara ◽  
Abdul Motaleb ◽  
Kyoji Horie ◽  
Toru Higashinakagawa ◽  
...  
Keyword(s):  
Dna Binding ◽  
Protein A ◽  
Binding Activity ◽  
Mouse Homologue ◽  
Dna Binding Activity

Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering

2017 ◽  
Vol 97 ◽  
pp. 503-512 ◽  
Author(s):  
Thiago V. Seraphim ◽  
Kelly P. Silva ◽  
Paulo R. Dores-Silva ◽  
Leandro R.S. Barbosa ◽  
Júlio C. Borges
Keyword(s):  
Structural Dynamics ◽  
Small Angle ◽  
Molecular Chaperone ◽  
Leishmania Braziliensis ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Reduced sulphydryl groups are required for DNA binding of Ku protein

1993 ◽  
Vol 293 (3) ◽  
pp. 769-774 ◽  
Author(s):  
W W Zhang ◽  
M Yaneva
Keyword(s):  
Dna Binding ◽  
Protein A ◽  
Binding Activity ◽  
Heat Inactivation ◽  
Cysteine Residues ◽  
Dna Binding Activity ◽  
Sulphydryl Groups ◽  
Ku Protein

The Ku protein, a DNA-binding complex that is composed of two subunits of 70 kDa and of 86 kDa, has been suggested to play a role in gene transcription. The dependence of the in vitro DNA-binding activity of affinity-purified Ku protein on reduced cysteine residues has been studied using sulphydryl-modifying agents. Inhibition of the DNA-binding activity was caused by alkylation with N-ethylmaleimide and by crosslinking with azadicarboxylic acid bis(dimethylamide). Treatment of the protein with a large excess of N-ethylmaleimide after it had bound to DNA did not completely dissociate the complex from the DNA, suggesting that some cysteines may be in direct contact with DNA. Pre-incubation of the protein at 37 degrees C or above caused rapid inactivation of DNA binding. The elevated temperature azadicarboxylic acid bis(dimethylamide) treatments resulted in the formation of a crosslinked product, which was detected by Western blotting. The effects of azadicarboxylic acid bis(dimethylmaleimide) and heat were completely reversible by treatment with a reducing agent, such as dithiothreitol. These results demonstrate that in vitro DNA-binding activity of the Ku protein requires reduced sulphydryl groups. Interestingly, the DNA-binding activity of Ku protein was protected from heat inactivation by the presence of a HeLa cell nuclear extract, suggesting that a nuclear factor or factors may be responsible for the maintenance of the reduced cysteines of the Ku protein in vivo. Thus, the biochemical function of the Ku protein may be regulated through oxidation-reduction of its cysteine residues.

Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein

1991 ◽  
Vol 11 (2) ◽  
pp. 765-772
Author(s):  
N Kamata ◽  
R M Jotte ◽  
J T Holt
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Biochemical Analysis ◽  
Protein A ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Fos Protein ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma

FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.

scholarly journals The Statistical Conformation of a Highly Flexible Protein: Small-Angle X-Ray Scattering of S. aureus Protein A

Structure ◽  
2014 ◽  
Vol 22 (8) ◽  
pp. 1184-1195 ◽  
Author(s):  
Jo A. Capp ◽  
Andrew Hagarman ◽  
David C. Richardson ◽  
Terrence G. Oas
Keyword(s):  
Small Angle ◽  
Protein A ◽  
X Ray ◽  
X Ray Scattering ◽  
Flexible Protein ◽  
Ray Scattering
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