The open and closed conformations are in dynamic equilibrium. In the closed conformation at low salt and swivels open at high salt in the absence of DNA. Our ensemble studies show that the 2B domain is To study the conformational changes of the 2Bĭomain, double cysteine mutants with one pair on 1B and 2B domains andĪnother pair on 2A and 2B domains were constructed and labeled with a mixture of donor-acceptor fluorophores such that the movement of 2B domain results in either an increase or a decrease in FRET, depending on the positions The rotational orientations of the 2B domain differ in these two UvrD can exist in two dramatically different conformations, ‘‘open’’ in theĪpo state and ‘‘closed’’ when forming a complex with a 30 - ssDNA-dsDNA The same directionality as used in unwinding. Single turnover pre-steady state DNA unwinding kinetics experiments have shown that the UvrD dimer is the active form of the helicase in vitro, although a UvrD monomer can translocate along ssDNA with (dsDNA) and translocate along single-stranded DNA (ssDNA) with biasedģ0 to 50 directionality. UvrD uses theĮnergy of ATP binding and hydrolysis to unwind double-stranded DNA That functions in nucleotide excision repair and methyl-directed mismatch repair of DNA, as well as DNA replication of certain plasmids. The Escherichia coli UvrD protein is a 30 to 50 superfamily 1 DNA helicase Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA. Washington University School of Medicine, St. Haifeng Jia1, Anita Niedziela-Majka1, Sergey Korolev2, Taekjip Ha3, Fret Studies of the Conformational Changes in the 2b Sub-Domain of
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