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An oligomeric form of E. coli UvrD is required for optimal helicase activity.

Abstract：

:Pre-steady-state chemical quenched-flow techniques were used to study DNA unwinding catalyzed by Escherichia coli UvrD helicase (helicase II), a member of the SF1 helicase superfamily. Single turnover experiments, with respect to unwinding of a DNA oligonucleotide, were used to examine the DNA substrate and UvrD concentration requirements for rapid DNA unwinding by pre-bound UvrD helicase. In excess UvrD at low DNA concentrations (1 nM), the bulk of the DNA is unwound rapidly by pre-bound UvrD complexes upon addition of ATP, but with time-courses that display a distinct lag phase for formation of fully unwound DNA, indicating that unwinding occurs in discrete steps, with a "step size" of four to five base-pairs as previously reported. Optimum unwinding by pre-bound UvrD-DNA complexes requires a 3' single-stranded (ss) DNA tail of 36-40 nt, whereas productive complexes do not form readily on DNA with 3'-tail lengths

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ali JA,Maluf NK,Lohman TM

doi

10.1006/jmbi.1999.3185

keywords:

subject

Has Abstract

pub_date

1999-11-05 00:00:00

pages

815-34

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)93185-6

journal_volume

293

pub_type

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