ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop

Journal of Molecular Biology
J DekkerP C van der Vliet

Abstract

The adenovirus DNA binding protein (DBP) binds cooperatively to single-stranded (ss) DNA and stimulates both initiation and elongation of DNA replication. DBP forms protein filaments via a C-terminal arm that hooks into a neighbouring molecule. This multimerization is the driving force for ATP-independent DNA unwinding by DBP during elongation. Another conserved part of DBP forms an unstructured flexible loop that is probably directly involved in contacting DNA. By making appropriate deletion mutants that do not distort the overall DBP structure, the influence of the C-terminal arm and the flexible loop on the kinetics of ssDNA binding and on DNA replication was studied. Employing surface plasmon resonance we show that both parts of the protein are required for high affinity binding. Deletion of the C-terminal arm leads to an extremely labile DBP-ssDNA complex indicating the importance of multimerization. The flexible loop is also required for optimal stability of the DBP-ssDNA complex, providing additional evidence that this region forms part of the ssDNA-binding surface of DBP. Both deletion mutants are still able to stimulate initiation of DNA replication but are defective in supporting elongation, which may be caused by the...Continue Reading

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Citations

Dec 24, 1998·Nucleic Acids Research·I Michalopoulos, R T Hay
Jun 12, 2003·Nucleic Acids Research·R N de JongP C van der Vliet
Dec 28, 1999·Journal of Molecular Recognition : JMR·D G Myszka
Nov 26, 2019·FEBS Letters·Matthew CharmanMatthew D Weitzman
Nov 23, 2006·Molecular Biology Reports·Rajneesh Kumar Gaur
Apr 6, 2001·Analytical Chemistry·F LisdatR Brigelius-Flohé
Oct 12, 2001·Biochemical and Biophysical Research Communications·K C DudasW T Ruyechan

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