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Literature DB >> 1864499

Escherichia coli RecBCD enzyme: inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunits.

Abstract

The intracellular levels of the Escherichia coli RecBCD proteins have been amplified by fusing the recBCD genes to the strong tac promoter/operator in the expression vector, pKK223-3. The overproduced proteins occur at levels amounting to approx. 10% of total cellular protein. Strains harbouring these overexpression plasmids have been used to purify the RecB. RecC and RecD protein subunits, as well as the RecBCD holoenzyme. The individually purified protein subunits can be used to reconstitute the ATP-dependent DNase activity of the RecBCD enzyme.

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Year: 1991 PMID： 1864499 DOI： 10.1016/0378-1119(91)90529-k

Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688

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Cited

10 in total

1. The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation.

Authors: J J Churchill; D G Anderson; S C Kowalczykowski
Journal: Genes Dev Date: 1999-04-01 Impact factor: 11.361

2. The 30-kDa C-terminal domain of the RecB protein is critical for the nuclease activity, but not the helicase activity, of the RecBCD enzyme from Escherichia coli.

Authors: M Yu; J Souaya; D A Julin
Journal: Proc Natl Acad Sci U S A Date: 1998-02-03 Impact factor: 11.205

3. A stimulatory RNA associated with RecBCD enzyme.

Authors: S K Amundsen; A F Taylor; G R Smith
Journal: Nucleic Acids Res Date: 1998-05-01 Impact factor: 16.971

4. In vivo studies on the interaction of RecBCD enzyme and lambda Gam protein.

Authors: N Marsić; S Roje; I Stojiljković; E Salaj-Smic; Z Trgovcević
Journal: J Bacteriol Date: 1993-08 Impact factor: 3.490

5. DNA replication triggered by double-stranded breaks in E. coli: dependence on homologous recombination functions.

Authors: T Asai; D B Bates; T Kogoma
Journal: Cell Date: 1994-09-23 Impact factor: 41.582

6. Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot chi in vitro: evidence for functional inactivation or loss of the RecD subunit.

Authors: D A Dixon; J J Churchill; S C Kowalczykowski
Journal: Proc Natl Acad Sci U S A Date: 1994-04-12 Impact factor: 11.205

Escherichia coli RecBCD enzyme: inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunits.

1. The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation.

2. The 30-kDa C-terminal domain of the RecB protein is critical for the nuclease activity, but not the helicase activity, of the RecBCD enzyme from Escherichia coli.

3. A stimulatory RNA associated with RecBCD enzyme.

4. In vivo studies on the interaction of RecBCD enzyme and lambda Gam protein.

5. DNA replication triggered by double-stranded breaks in E. coli: dependence on homologous recombination functions.

6. Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot chi in vitro: evidence for functional inactivation or loss of the RecD subunit.

Review 7. Biochemistry of homologous recombination in Escherichia coli.

8. Regulation of homologous recombination: Chi inactivates RecBCD enzyme by disassembly of the three subunits.

Review 9. Functions of the gene products of Escherichia coli.

10. Control of RecBCD enzyme activity by DNA binding- and Chi hotspot-dependent conformational changes.