A Eukaryotic SWI2/SNF2 Domain, an Exquisite Detector of Double-stranded to Single-stranded DNA Transition Elements

• Published in: The Journal of biological chemistry 2000-03, Vol.275 (11), p.7648-7655
• Main Authors: Muthuswami, Rohini, Truman, Patrick A., Mesner, Larry D., Hockensmith, Joel W.
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - classification; Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Binding Sites; DNA - chemistry; DNA - metabolism; DNA Helicases; DNA, Single-Stranded - chemistry; DNA, Single-Stranded - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - classification; DNA-Binding Proteins - metabolism; Eukaryotic Cells; Molecular Motor Proteins - chemistry; Molecular Motor Proteins - classification; Molecular Motor Proteins - metabolism; Molecular Sequence Data; Nuclear Proteins; Nucleic Acid Conformation; Protein Binding; Protein Structure, Tertiary; Sequence Analysis, Protein; SWI2/SNF2 protein; Transcription Factors - classification
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.275.11.7648

Many members of the SWI2/SNF2 family of adenosine triphosphatases participate in the assembly/disassembly of multiprotein complexes involved in the DNA metabolic processes of transcription, recombination, repair, and chromatin remodeling. The DNA molecule serves as an essential effector or catalyst for most of the members of this particular class of proteins, and the structure of the DNA may be more important than the nucleotide sequence. Inspection of the DNA structure at sites where multiprotein complexes are assembled/disassembled for these various DNA metabolic processes reveals the presence of a common element: a double-stranded to single-stranded transition region. We now show that this DNA element is crucial for the ATP hydrolytic function of an SWI2/SNF2 family member: DNA-dependent ATPase A. We further demonstrate that a domain containing the seven helicase-related motifs that are common to the SWI2/SNF2 family of proteins mediates the interaction with the DNA, yielding specific DNA structural recognition. This study forms a primary step toward understanding the physico-biochemical nature of the interaction between a particular class of DNA-dependent ATPase and their DNA effectors. Furthermore, this study provides a foundation for development of mechanisms to specifically target this class of DNA-dependent ATPases.