Characterization of the DNA binding domain of bacteriophage lambda O protein.
نویسندگان
چکیده
منابع مشابه
Characterization of the integration protein of bacteriophage lambda as a site-specific DNA-binding protein.
The Int protein specified by bacteriophage lambda is required for the recombination event that integrates the viral DNA into the host genome at its specific attachment site. Using a DNA-binding assay, we have partially purified the Int protein and studied some of the features of its binding specificity and regulation. The DNA-binding activity is attributed to Int protein because the activity is...
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The bacteriophage lambda excisionase (Xis) is a sequence-specific DNA binding protein required for excisive recombination. Xis binds cooperatively to two DNA sites arranged as direct repeats on the phage DNA. Efficient excision is achieved through a cooperative interaction between Xis and the host-encoded factor for inversion stimulation as well as a cooperative interaction between Xis and inte...
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Introduction: P53 is a tumor suppressor protein with numerous missense mutations identified in its gene. These mutations are observed in a vast number of cancers. R213G is one of them which has a role in metastatic lung cancers. In this research, R213G was studied in comparison with the wild type via molecular dynamics simulation. Method: For the three-dimensional structure of the wild-type P53...
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متن کاملNucleotide sequence of the O gene and of the origin of replication in bacteriophage lambda DNA.
The nucleotide sequence of the O gene in bacteriophage lambda DNA is presented. According to two possible initiator codons, the primary structure of the O protein deduced from the DNA sequence consists of 278 or 299 amino acid residues. Structure and function of the O protein--one of the two phage initiator proteins for lambda DNA replication--are discussed in the light of a secondary structure...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)38425-9