Crystal structure of the P2 C-repressor: a binder of nonpalindromic direct DNA repeats

Crystal structure of the P2 C-repressor : a binder of nonpalindromic direct DNA repeats

Massad, Tariq (author): Stockholms universitet,Institutionen för biokemi och biofysik

Skaar, Karin (author): Stockholms universitet,Institutionen för biokemi och biofysik

Nilsson, Hanna (author): Stockholms universitet,Institutionen för genetik, mikrobiologi och toxikologi

Damberg, Peter (author): Stockholms universitet,Institutionen för biokemi och biofysik

Henriksson-Peltola, Petri (author): Stockholms universitet,Institutionen för genetik, mikrobiologi och toxikologi

Haggård-Ljungquist, Elisabeth (author): Stockholms universitet,Institutionen för genetik, mikrobiologi och toxikologi

Högbom, Martin (author): Stockholms universitet,Institutionen för biokemi och biofysik

Stenmark, Pål (author): Stockholms universitet,Institutionen för biokemi och biofysik

(creator_code:org_t)

2010-07-17
2010
English.
In: Nucleic Acids Research. - : Oxford University Press (OUP). - 0305-1048 .- 1362-4962. ; 38:21, s. 7778-7790

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Abstract Subject headings

As opposed to the vast majority of prokaryoticrepressors, the immunity repressor of temperateEscherichia coli phage P2 (C) recognizes nonpalindromicdirect repeats of DNA rather thaninverted repeats. We have determined the crystalstructure of P2 C at 1.8A ° . This constitutes the firststructure solved from the family of C proteins fromP2-like bacteriophages. The structure reveals thatthe P2 C protein forms a symmetric dimer orientedto bind the major groove of two consecutive turns ofthe DNA. Surprisingly, P2 C has great similarities tobinders of palindromic sequences. Nevertheless, thetwo identical DNA-binding helixes of the symmetricP2 C dimer have to bind different DNA sequences.Helix 3 is identified as the DNA-recognition motif inP2 C by alanine scanning and the importance for theindividual residues in DNA recognition is defined.A truncation mutant shows that the disorderedC-terminus is dispensable for repressor function.The short distance between the DNA-bindinghelices together with a possible interaction betweentwo P2 C dimers are proposed to be responsible forextensive bending of the DNA. The structure providesinsight into the mechanisms behind the mutants ofP2 C causing dimer disruption, temperature sensitivityand insensitivity to the P4 antirepressor.

By the author/editor: Massad, Tariq; Skaar, Karin; Nilsson, Hanna; Damberg, Peter; Henriksson-Pelto ...; Haggård-Ljungqui ...; show more...; Högbom, Martin; Stenmark, Pål; show less...

About the subject

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Structural Biolo ...

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