Homo-oligomerization Is the Essential Function of the Tandem BRCT Domains in the Checkpoint Protein Crb2.

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Title: Homo-oligomerization Is the Essential Function of the Tandem BRCT Domains in the Checkpoint Protein Crb2.
Authors: Li-Lin Du1, Moser, Bettina A.1, Russell, Paul1 prussell@scripps.edu
Source: Journal of Biological Chemistry. 9/10/2004, Vol. 279 Issue 37, p38409-38414. 6p. 30 Black and White Photographs, 1 Chart, 3 Graphs.
Subjects: Proteins, DNA damage, Genes, Nucleic acids, Genetic mutation, Biochemical genetics, Saccharomyces cerevisiae
Abstract: BRCT (BRCA1 C terminus) domains are frequently found as a tandem repeat in proteins involved in DNA damage responses, such as Saccharomyces cerevisiae Rad9, human 53BP1 and BRCA1. Tandem BRCT domains mediate protein-protein and protein-DNA interactions. However, the functional significance of these interactions is largely unknown. Here we report the oligomerization of Schizosaccharomyces pombe checkpoint protein Crb2 through its tandem BRCT domains. Truncated Crb2 without BRCT domains is defective in DNA damage checkpoint signaling. However, addition of either of two heterologous dimerization motifs largely restores the functions of truncated Crb2 without BRCT domains. Replacement of Crb2 BRCT domains with a dimerization motif also renders cells resistant to the dominant negative effect of overexpressing Crb2 BRCT domains. These results demonstrate that the crucial function of the tandem BRCT domains is to oligomerize Crb2. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Homo-oligomerization Is the Essential Function of the Tandem BRCT Domains in the Checkpoint Protein Crb2.
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  Data: <searchLink fieldCode="AR" term="%22Li-Lin+Du%22">Li-Lin Du</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Moser%2C+Bettina+A%2E%22">Moser, Bettina A.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Russell%2C+Paul%22">Russell, Paul</searchLink><relatesTo>1</relatesTo><i> prussell@scripps.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 9/10/2004, Vol. 279 Issue 37, p38409-38414. 6p. 30 Black and White Photographs, 1 Chart, 3 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22DNA+damage%22">DNA damage</searchLink><br /><searchLink fieldCode="DE" term="%22Genes%22">Genes</searchLink><br /><searchLink fieldCode="DE" term="%22Nucleic+acids%22">Nucleic acids</searchLink><br /><searchLink fieldCode="DE" term="%22Genetic+mutation%22">Genetic mutation</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemical+genetics%22">Biochemical genetics</searchLink><br /><searchLink fieldCode="DE" term="%22Saccharomyces+cerevisiae%22">Saccharomyces cerevisiae</searchLink>
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  Data: BRCT (BRCA1 C terminus) domains are frequently found as a tandem repeat in proteins involved in DNA damage responses, such as Saccharomyces cerevisiae Rad9, human 53BP1 and BRCA1. Tandem BRCT domains mediate protein-protein and protein-DNA interactions. However, the functional significance of these interactions is largely unknown. Here we report the oligomerization of Schizosaccharomyces pombe checkpoint protein Crb2 through its tandem BRCT domains. Truncated Crb2 without BRCT domains is defective in DNA damage checkpoint signaling. However, addition of either of two heterologous dimerization motifs largely restores the functions of truncated Crb2 without BRCT domains. Replacement of Crb2 BRCT domains with a dimerization motif also renders cells resistant to the dominant negative effect of overexpressing Crb2 BRCT domains. These results demonstrate that the crucial function of the tandem BRCT domains is to oligomerize Crb2. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1074/jbc.M403326200
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      – Code: eng
        Text: English
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        StartPage: 38409
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        Type: general
      – SubjectFull: DNA damage
        Type: general
      – SubjectFull: Genes
        Type: general
      – SubjectFull: Nucleic acids
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      – SubjectFull: Genetic mutation
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      – SubjectFull: Biochemical genetics
        Type: general
      – SubjectFull: Saccharomyces cerevisiae
        Type: general
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      – TitleFull: Homo-oligomerization Is the Essential Function of the Tandem BRCT Domains in the Checkpoint Protein Crb2.
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            NameFull: Li-Lin Du
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            NameFull: Moser, Bettina A.
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              M: 09
              Text: 9/10/2004
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              Y: 2004
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              Value: 37
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