Analysis of the mammalian recombination protein complex RC-1

Rolf Jessberger; Gloria Chui; Stuart Linn; Börries Kemper

doi:10.1016/0027-5107(95)00106-9

Analysis of the mammalian recombination protein complex RC-1

Rolf Jessberger, Gloria Chui, Stuart Linn, Börries Kemper

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Based on a novel cell-free assay for DNA recombination, we previously reported the purification and initial characterization of RC-1, a protein complex catalyzing the recombinational repair of deletions and gaps. RC-1 was isolated from calf thymus nuclear extracts and shown to copurify with several enzymatic activities, among them a DNA polymerase. Here, additional evidence is reported identifying the polymerase as DNA polymerase ε. Furthermore, a novel DNA structure-dependent endonuclease associated with RC-1 was observed, which recognizes and cleaves branched DNA substrates at specific sites. Implications of this endonuclease activity for the recombination reaction are discussed.

Original language	English
Pages (from-to)	217-227
Number of pages	11
Journal	Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
Volume	350
Issue number	1
DOIs	https://doi.org/10.1016/0027-5107(95)00106-9
State	Published - 19 Feb 1996
Externally published	Yes

Keywords

DNA polymerase ε
RC-1 endonuclease
Recombination

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10.1016/0027-5107(95)00106-9

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title = "Analysis of the mammalian recombination protein complex RC-1",

abstract = "Based on a novel cell-free assay for DNA recombination, we previously reported the purification and initial characterization of RC-1, a protein complex catalyzing the recombinational repair of deletions and gaps. RC-1 was isolated from calf thymus nuclear extracts and shown to copurify with several enzymatic activities, among them a DNA polymerase. Here, additional evidence is reported identifying the polymerase as DNA polymerase ε. Furthermore, a novel DNA structure-dependent endonuclease associated with RC-1 was observed, which recognizes and cleaves branched DNA substrates at specific sites. Implications of this endonuclease activity for the recombination reaction are discussed.",

keywords = "DNA polymerase ε, RC-1 endonuclease, Recombination",

author = "Rolf Jessberger and Gloria Chui and Stuart Linn and B{\"o}rries Kemper",

note = "Funding Information: The authors wish to thank Drs. Hans-Reimer Rodewald and Jean-Marie Buerstedde for critical reading the manuscript, and V. Illner-Brbtigam (Cologne) for expert technical assistance.T he Base1 Institute is founded and supported by Hoffman-LaRoche Inc., Basel. Work in Cologne was funded by the Deutsche Forschungsgemeinschaftt hrough SFB 274. Work in Berkeley was funded by Grants RO I -GM304 IS, P30ESO1 1896, and T32ES07075 from the USPHS.",

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doi = "10.1016/0027-5107(95)00106-9",

language = "English",

volume = "350",

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T1 - Analysis of the mammalian recombination protein complex RC-1

AU - Jessberger, Rolf

AU - Chui, Gloria

AU - Linn, Stuart

AU - Kemper, Börries

N1 - Funding Information: The authors wish to thank Drs. Hans-Reimer Rodewald and Jean-Marie Buerstedde for critical reading the manuscript, and V. Illner-Brbtigam (Cologne) for expert technical assistance.T he Base1 Institute is founded and supported by Hoffman-LaRoche Inc., Basel. Work in Cologne was funded by the Deutsche Forschungsgemeinschaftt hrough SFB 274. Work in Berkeley was funded by Grants RO I -GM304 IS, P30ESO1 1896, and T32ES07075 from the USPHS.

PY - 1996/2/19

Y1 - 1996/2/19

N2 - Based on a novel cell-free assay for DNA recombination, we previously reported the purification and initial characterization of RC-1, a protein complex catalyzing the recombinational repair of deletions and gaps. RC-1 was isolated from calf thymus nuclear extracts and shown to copurify with several enzymatic activities, among them a DNA polymerase. Here, additional evidence is reported identifying the polymerase as DNA polymerase ε. Furthermore, a novel DNA structure-dependent endonuclease associated with RC-1 was observed, which recognizes and cleaves branched DNA substrates at specific sites. Implications of this endonuclease activity for the recombination reaction are discussed.

AB - Based on a novel cell-free assay for DNA recombination, we previously reported the purification and initial characterization of RC-1, a protein complex catalyzing the recombinational repair of deletions and gaps. RC-1 was isolated from calf thymus nuclear extracts and shown to copurify with several enzymatic activities, among them a DNA polymerase. Here, additional evidence is reported identifying the polymerase as DNA polymerase ε. Furthermore, a novel DNA structure-dependent endonuclease associated with RC-1 was observed, which recognizes and cleaves branched DNA substrates at specific sites. Implications of this endonuclease activity for the recombination reaction are discussed.

KW - DNA polymerase ε

KW - RC-1 endonuclease

KW - Recombination

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JF - Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis

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ER -

Analysis of the mammalian recombination protein complex RC-1

Abstract

Keywords

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