Measurement of DNA helical change for the binding of cyclic AMP receptor protein to lac DNA.
Cyclic AMP receptor protein (CRP) binds to DNA and induces DNA bending. DNA bending plays an important role in transcription activation of many genes in Escherichia coli. To know DNA helical change by CRP, we used molar cyclization factor (j(M)), which is sensitive to helical twist or torsional alignment. Six consecutive DNA fragments were constructed that contained phasing sequence at left arm and CRP binding site in center. j(M) values measured in this study were approximately 10 times increased by CRP relative to that measured for DNA only. The analysis of set of j(M) values indicated that CRP induced DNA bending without the helical change like helical twisting or torsional alignment change.
Gang
JongBack
J
Department of Chemistry, Kyungwon University, Sungnam, Republic of Korea. jbgang@kyungwon.ac.kr
D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics*; D007763:Lac Operon; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011953:Receptors, Cyclic AMP / Q000378:metabolism*; D012044:Regression Analysis
D011953:Receptors, Cyclic AMP; D004247:DNA