Abstract：
:As opposed to the vast majority of prokaryotic repressors, the immunity repressor of temperate Escherichia coli phage P2 (C) recognizes non-palindromic direct repeats of DNA rather than inverted repeats. We have determined the crystal structure of P2 C at 1.8 Å. This constitutes the first structure solved from the family of C proteins from P2-like bacteriophages. The structure reveals that the P2 C protein forms a symmetric dimer oriented to bind the major groove of two consecutive turns of the DNA. Surprisingly, P2 C has great similarities to binders of palindromic sequences. Nevertheless, the two identical DNA-binding helixes of the symmetric P2 C dimer have to bind different DNA sequences. Helix 3 is identified as the DNA-recognition motif in P2 C by alanine scanning and the importance for the individual residues in DNA recognition is defined. A truncation mutant shows that the disordered C-terminus is dispensable for repressor function. The short distance between the DNA-binding helices together with a possible interaction between two P2 C dimers are proposed to be responsible for extensive bending of the DNA. The structure provides insight into the mechanisms behind the mutants of P2 C causing dimer disruption, temperature sensitivity and insensitivity to the P4 antirepressor.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Massad T,Skaar K,Nilsson H,Damberg P,Henriksson-Peltola P,Haggård-Ljungquist E,Högbom M,Stenmark Pdoi
10.1093/nar/gkq626subject
Has Abstractpub_date
2010-11-01 00:00:00pages
7778-90issue
21eissn
0305-1048issn
1362-4962pii
gkq626journal_volume
38pub_type
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