Dimerization specificity of P22 and 434 repressors is determined by multiple polypeptide segments.

doi:10.1128/jb.179.4.1253-1261.1997

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Article

Dimerization specificity of P22 and 434 repressors is determined by multiple polypeptide segments.

Journal of bacteriology - 1 Feb 1997

Donner A L, Carlson P A, Koudelka G B

Abstract excerpt

The repressor protein of bacteriophage P22 binds to DNA as a homodimer. This dimerization is absolutely required for DNA binding. Dimerization is mediated by interactions between amino acids in the carboxyl (C)-terminal domain. We have constructed a plasmid, p22CT-1, which directs the overproduct...

Topics

Amino Acid Sequence
Binding Sites
DNA Footprinting
Deoxyribonuclease I
Dimerization
Escherichia coli
Molecular Sequence Data
Mutation
Operator Regions, Genetic
Plasmids
Recombinant Fusion Proteins
Repressor Proteins
Viral Proteins

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