(Q54561850)

1 June 2018

title

Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect. (English)

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1 June 2018

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Hall MC

1

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1 June 2018

Matson SW

series ordinal

2

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1 June 2018

language of work or name

English

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publication date

1 July 1997

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1 June 2018

Journal of Biological Chemistry

published in

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1 June 2018

volume

272

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1 June 2018

issue

30

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1 June 2018

page(s)

18614-18620

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1 June 2018

D-E-A-D protein family of putative RNA helicases

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Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction

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Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase

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A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo.

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21 January 2018

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A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.272.30.18614

1 reference

1 June 2018

1 reference

1 June 2018