Colocalization, Physical, and Functional Interaction between Werner and Bloom Syndrome Proteins

• Published in: The Journal of biological chemistry Vol. 277; no. 24; pp. 22035 - 22044
• Main Authors: von Kobbe, Cayetano, Karmakar, Parimal, Dawut, Lale, Opresko, Patricia, Zeng, Xianmin, Brosh, Jr, Robert M, Hickson, Ian D, Bohr, Vilhelm A
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 14.06.2002
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; BLM protein; Bloom's syndrome; Blotting, Western; Cell Line; Cell Nucleus - metabolism; DNA Helicases - chemistry; DNA Helicases - metabolism; Enzyme-Linked Immunosorbent Assay; Exodeoxyribonucleases; HeLa Cells; Humans; Microscopy, Fluorescence; Models, Biological; Phenotype; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins - metabolism; RecQ Helicases; RecQ protein; Werner Syndrome Helicase; Werner's syndrome; WRN protein

The RecQ helicase family comprises a conserved group of proteins implicated in several aspects of DNA metabolism. Three of the family members are defective in heritable diseases characterized by abnormal growth, premature aging, and predisposition to malignancies. These include the WRN and BLM gene...