ANALYSIS OF THE DNA :BINDING PROPERTIES OF BACTERIOPHAGE P1 Cl REPRESSOR AND BOF MODULATOR PROTEINS 'UTILIZING A COMPARATIVE SELEX TECHNIQUE
Loading...
Links to Files
Permanent Link
Author/Creator
Author/Creator ORCID
Date
2001-03
Department
Hood College Biology
Program
Biomedical and Environmental Science
Citation of Original Publication
Rights
Subjects
Abstract
Bacteriophage P1 cycles between lytic and lysogenic states upon
infection of a host bacteria. P1 maintains its lysogenic stage by suppressing
gene expression from several lytic genes. Bacteriophage P1 C1 repressor protein
binds to a family of operator sequences to regulate gene expression. Protein
binding to these operator sites is regulated in a unique way by the P1 Bof
protein. Bof protein enhances the DNA binding capability of C1 repressor by
forming a ternary complex with Cl repressor and its cognate DNA. These DNA
binding interactions are characterized by looking at the variability in C1
repressor binding sites utilizing a partially randomized oligonucleotide library
based on a sequence logo constructed from an alignment of the natural C1
Operator sites and recombinant GST(glutathione S-Transferase) fusion C1
repressor and Bof proteins for SELEX (Systematic Evolution of Ligands by
Exponential enrichment) experiments. The consensus sequence of
oligonucleotides selected is A6TTGCICTAATA5. Palindromes are not
important for binding, as previously hypothesized. A different hypothesis,
emphasizing the role of DNA bending is discussed.