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Literature DB >> 199440

DNA unwinding enzyme II of Escherichia coli. 1. Purification and characterization of the ATPase activity.

M Abdel-Monem, M C Chanal, H Hoffmann-Berling.

Abstract

A DNA-stimulated ATP-gamma-phosphohydrolase of molecular weight 75000 was purified from Escherichia coli cells. The ATPase, a globular molecule (identical probably with an ATPase described previously by Richet and Kohiyama in 1976) shows specificity for adenine nucleotides, it prefers single-stranded DNA as the cofactor, it exhibits a complicated mode of response to variations of the cofacter concentration and it is devoid of nuclease activity. Preparations derived from rep3 mutant cells yield widely varying amounts of an apparently normal ATPase.

Entities: Chemical Gene Species

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Year: 1977 PMID： 199440 DOI： 10.1111/j.1432-1033.1977.tb11780.x

Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956

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Cited

18 in total

1. Modulation of UvrD helicase activity by covalent DNA-protein cross-links.

Authors: Anuradha Kumari; Irina G Minko; Rebecca L Smith; R Stephen Lloyd; Amanda K McCullough
Journal: J Biol Chem Date: 2010-05-04 Impact factor: 5.157

2. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke.

Authors: Jae Young Lee; Wei Yang
Journal: Cell Date: 2006-12-29 Impact factor: 41.582

3. Identification and characterization of Escherichia coli DNA helicase II mutants that exhibit increased unwinding efficiency.

Authors: G Zhang; E Deng; L Baugh; S R Kushner
Journal: J Bacteriol Date: 1998-01 Impact factor: 3.490

4. Escherichia coli DNA helicase II (uvrD gene product) catalyzes the unwinding of DNA.RNA hybrids in vitro.

Authors: S W Matson
Journal: Proc Natl Acad Sci U S A Date: 1989-06 Impact factor: 11.205

5. Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.

Authors: A O Adedeji; K Singh; S G Sarafianos
Journal: Cell Mol Biol (Noisy-le-grand) Date: 2012-12-22 Impact factor: 1.770

6. Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the uvrABC protein complex.

Authors: P R Caron; S R Kushner; L Grossman
Journal: Proc Natl Acad Sci U S A Date: 1985-08 Impact factor: 11.205

DNA unwinding enzyme II of Escherichia coli. 1. Purification and characterization of the ATPase activity.

1. Modulation of UvrD helicase activity by covalent DNA-protein cross-links.

2. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke.

3. Identification and characterization of Escherichia coli DNA helicase II mutants that exhibit increased unwinding efficiency.

4. Escherichia coli DNA helicase II (uvrD gene product) catalyzes the unwinding of DNA.RNA hybrids in vitro.

5. Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.

6. Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the uvrABC protein complex.

7. Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease.

8. The E. coli uvrD gene product is DNA helicase II.

9. Three deoxyribonucleic acid-dependent adenosine triphosphatases from Bacillus subtilis.

10. Properties of a DNA-dependent ATPase from rat mitochondria.