Monoclonal antibodies and mechanistic studies on recA protein

Shibata, Takehiko; Ikeda, Masayuki; Makino, Osamu; Ikawa, Shiro

doi:10.1016/0300-9084(91)90204-e

Biochimie

1991

DOI: 10.1016/0300-9084(91)90204-e

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Monoclonal antibodies and mechanistic studies on recA protein

Takehiko Shibata

Masayuki Ikeda

Osamu Makino

et al.

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Cited by 3 publications

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“…To this end, we have adapted the approach taken by Shibata and colleagues with RecA (reviewed in Shibata et al, 1991) using monoclonal antibodies directed against Sepl. Here, we show that, from a panel of 12 anti-Sepl mAbs, four specifically inhibited the in vitro homologous pairing activity of Sepl.…”

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confidence: 99%

Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

Holler

Bashkirov

Solinger

et al. 1995

European Journal of Biochemistry

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The Saccharomyces cerevisiae strand-exchange protein 1 (Sepl also known as Xml, Keml, Rar.5, StppIDST2) has been demonstrated to mediate the formation of hybrid DNA from model substrates of linear double-stranded and circular single-stranded DNA in v i m . To delineate the mechanism by which Sepl acts in the strand-exchange reaction, we analyzed mouse anti-Sepl monoclonal antibodies for inhibition of the Sepl in vitro activity. Of 12 class-G immunoglobulins tested, four were found to consistently inhibit the Sepl-mediated strand-exchange reaction. The inhibiting antibodies were tested for inhibition of a variety of Sepl -catalyzed DNA reactions including exonuclease activity on double-stranded and single-stranded DNA, renaturation of complementary single-stranded DNA and condensation of DNA into large aggregates. All four inhibiting antibodies had no effect on the exonuclease activity of Sepl. Three antibodies specifically blocked DNA aggregation. In addition, one antibody inhibited renaturation of complementary single-stranded DNA. This inhibition pattern underlines the importance of condensation of DNA into large aggregates in conjunction with double-stranded DNA exonuclease activity for the in vitro homologous pairing activity of Sepl. The implications of these data for the interpretation of proteins which promote homologous pairing of DNA are discussed, in particular in light of the reannealing activity of the p53 human tumor-suppressor protein.

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mentioning

confidence: 99%

Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

Holler

Bashkirov

Solinger

et al. 1995

European Journal of Biochemistry

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Epitope mapping of anti-recA protein IgGs by region specified polymerase chain reaction mutagenesis.

Ikeda

Hamano

Shibata

1992

Journal of Biological Chemistry

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Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

Holler¹,

Bashkirov²,

Solinger³

et al. 1995

Eur J Biochem

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The Saccharomyces cerevisiae strand-exchange protein 1 (Sep1 also known as Xrn1, Kem1, Rar5, Stp beta/DST2) has been demonstrated to mediate the formation of hybrid DNA from model substrates of linear double-stranded and circular single-stranded DNA in vitro. To delineate the mechanism by which Sep1 acts in the strand-exchange reaction, we analyzed mouse anti-Sep1 monoclonal antibodies for inhibition of the Sep1 in vitro activity. Of 12 class-G immunoglobulins tested, four were found to consistently inhibit the Sep1-mediated strand-exchange reaction. The inhibiting antibodies were tested for inhibition of a variety of Sep1-catalyzed DNA reactions including exonuclease activity on double-stranded and single-stranded DNA, renaturation of complementary single-stranded DNA and condensation of DNA into large aggregates. All four inhibiting antibodies had no effect on the exonuclease activity of Sep1. Three antibodies specifically blocked DNA aggregation. In addition, one antibody inhibited renaturation of complementary single-stranded DNA. This inhibition pattern underlines the importance of condensation of DNA into large aggregates in conjunction with double-stranded DNA exonuclease activity for the in vitro homologous pairing activity of Sep1. The implications of these data for the interpretation of proteins which promote homologous pairing of DNA are discussed, in particular in light of the reannealing activity of the p53 human tumor-suppressor protein.

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Monoclonal antibodies and mechanistic studies on recA protein

Cited by 3 publications

References 40 publications

Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

Epitope mapping of anti-recA protein IgGs by region specified polymerase chain reaction mutagenesis.

Use of Monoclonal Antibodies in the Functional Characterization of the Saccharomyces Cerevisiae Sepl Protein

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