Quantitative analysis of the transcription factor AP2 binding to DNA by atomic force microscopy.
Atomic force microscopy (AFM) allows to study the molecular structure of biological macromolecules with nm to A resolutions without crystallization. We show here the applicability of AFM in the quantitative analysis of the molecular mechanisms of DNA/protein interaction: (i) Protein-binding sites can be mapped over a few kilobases of target DNA. (ii) Multimerization state of DNA-binding proteins can be determined simply by measuring the sizes of proteins bound to the DNA. These features are significant advantages over the capabilities provided by conventional techniques in biochemistry and molecular and structural biology.
Nettikadan
S
S
Department of Medical Biochemistry, Ohio State University, Columbus 43210, USA.
Tokumasu
F
F
Takeyasu
K
K
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D018625:Microscopy, Atomic Force / Q000379:methods; D008958:Models, Molecular; D011485:Protein Binding; D012044:Regression Analysis; D000254:Sodium-Potassium-Exchanging ATPase / Q000235:genetics; D016329:Sp1 Transcription Factor / Q000737:chemistry / Q000378:metabolism; D050656:Transcription Factor AP-2; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*
D004268:DNA-Binding Proteins; D016329:Sp1 Transcription Factor; D050656:Transcription Factor AP-2; D014157:Transcription Factors; D004247:DNA; D000254:Sodium-Potassium-Exchanging ATPase