Synthesis and mass spectrometric characterisation of the N-terminal (1-63) DNA-binding domain of the bacteriophage 434 repressor cI

1997 ◽  
Vol 3 (1) ◽  
pp. 151
Author(s):  
Piergiorgio Percipalle ◽  
Sandor Pongor ◽  
Sotir Zakhariev ◽  
Corrado Guarnaccia ◽  
Rosaria Saletti ◽  
...  
Keyword(s):  
Dna Binding ◽  
Mass Spectrometric ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Bacteriophage 434 ◽  
Bacteriophage 434 Repressor ◽  
434 Repressor

Structural Role of a Buried Salt Bridge in the 434 Repressor DNA-binding Domain

1996 ◽  
Vol 264 (5) ◽  
pp. 1002-1012 ◽  
Author(s):  
Konstantin Pervushin ◽  
Martin Billeter ◽  
Gregg Siegal ◽  
Kurt Wüthrich
Keyword(s):  
Dna Binding ◽  
Salt Bridge ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Structural Role ◽  
434 Repressor

Mass Spectrometric Analysis of a Native Zinc-Finger Structure: The Glucocorticoid Receptor DNA Binding Domain. [Erratum to document cited in CA122:233711]

1995 ◽  
Vol 117 (28) ◽  
pp. 7582-7582
Author(s):  
H. Ewa Witkowska ◽  
Cedric H. L. Shackleton ◽  
Karin Dahlman-Wright ◽  
John Y. Kim ◽  
Jan-Aake Gustafsson
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Zinc Finger ◽  
Mass Spectrometric ◽  
Binding Domain ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Dna Binding Domain

scholarly journals Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator.

1984 ◽  
Vol 81 (5) ◽  
pp. 1307-1311 ◽  
Author(s):  
J. Anderson ◽  
M. Ptashne ◽  
S. C. Harrison
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
434 Repressor

scholarly journals The Preferred Substrate for RecA-Mediated Cleavage of Bacteriophage 434 Repressor Is the DNA-Bound Dimer

2004 ◽  
Vol 186 (1) ◽  
pp. 1-7 ◽  
Author(s):  
David R. Pawlowski ◽  
Gerald B. Koudelka
Keyword(s):  
Dna Binding ◽  
Transcriptional Regulatory ◽  
Dna Binding Site ◽  
Cleavage Step ◽  
Regulatory Functions ◽  
Bacteriophage 434 ◽  
Dna Complex ◽  
Bacteriophage 434 Repressor ◽  
434 Repressor

ABSTRACT Induction of a lysogen of a lambdoid bacteriophage usually involves RecA-stimulated autoproteolysis of the bacteriophage repressor protein. Previous work on the phage repressors showed that the monomeric form of the protein is the target of RecA. Our previous work indicated that in the case of bacteriophage 434, virtually none of the repressor is present as a monomer in vivo. Hence, if the repressor in a lysogen is present as a dimer, how can RecA-stimulated autoproteolysis play a role in bacteriophage induction? We examined this question by determining the rate of RecA-stimulated 434 repressor cleavage as a function of repressor concentration and added DNA. Our results show that binding of 434 repressor to a specific DNA binding site dramatically increases the velocity of repressor autocleavage compared to the velocity of cleavage of the monomer and concentration-induced dimer. DNA binding-deficient hemidimers formed between the intact repressor and its C-terminal domain fragment have a lower rate of cleavage than DNA-bound dimers. These results show that the DNA-bound 434 repressor dimer, which is the form of the repressor that is required for its transcriptional regulatory functions, is the preferred form for RecA-stimulated autocleavage. We also show that the rate of repressor autocleavage is influenced by the sequence of the bound DNA. Kinetic analysis of the autocleavage reaction indicated that the DNA sequence influences the velocity of 434 repressor autocleavage by affecting the affinity of the repressor-DNA complex for RecA, not the chemical cleavage step. Regardless of the mechanism, the finding that the presence and precise sequence of DNA modulate the autocleavage reaction shows that DNA allosterically affects the function of 434 repressor.

scholarly journals Interaction of urea with an unfolded protein The DNA-binding domain of the 434-repressor

FEBS Letters ◽  
1995 ◽  
Vol 366 (1) ◽  
pp. 6-10 ◽  
Author(s):  
V. Dötsch ◽  
G. Wider ◽  
G. Siegal ◽  
K. Wüthrich
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Unfolded Protein ◽  
434 Repressor
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