How Trp repressor binds to its operator.
AUTOR(ES)
Staacke, D
RESUMO
We propose that the generally accepted model of a single Trp repressor dimer binding to a center of symmetry in the natural trp operator (Otwinowski et al., 1988) is wrong. We show here that the Trp repressor binds to a sequence whose center is located four base pairs either to the right or to the left of the central axis of symmetry that was previously identified. We show that: (i) the oligonucleotide used by Otwinowski et al. is not retarded by the Trp repressor in a mobility shift assay under conditions wherein a shorter oligonucleotide carrying our consensus sequence is retarded, (ii) that methylation protection experiments on the full natural operator sequence and the short oligonucleotide protect similar patterns and (iii) that by varying every base in the shorter oligonucleotide, we can demonstrate an optimal sequence for Trp repressor binding.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=551905Documentos Relacionados
- How Trp repressor binds to its operator.
- A repressor heterodimer binds to a chimeric operator.
- How lac repressor recognizes lac operator.
- Lac repressor with the helix-turn-helix motif of lambda cro binds to lac operator.
- Yeast repressor alpha 2 binds to its operator cooperatively with yeast protein Mcm1.
