The BRCT Regions of Tumor Suppressor BRCA1 and of XRCC1 Show DNA End Binding Activity with a Multimerizing Feature

Yamane, Kunio; Katayama, Eisaku; Tsuruo, Takashi

doi:10.1006/bbrc.2000.3983

Cited by 57 publications

(57 citation statements)

References 27 publications

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“…Similarly, an 18-amino acid stretch with five positive charges is present at the N-terminal BRCT domain of hRap1 (10). This is consistent with the finding of a single BRCT domain involved in the DNA binding of TopBP1 (42), XRCC1 (43) and replication factor C (44) to ds-ss junctions. Thus, the BRCT domain of hRap1 may account for its binding to these ds-ss junctions.…”

Section: Discussionsupporting

confidence: 91%

Human Rap1 Interacts Directly with Telomeric DNA and Regulates TRF2 Localization at the Telomere

Arat

Griffith

2012

Journal of Biological Chemistry

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Background: hTRF2 and hRap1 prevent non-homologous end joining and exist as a complex at human telomeres. Results: The TRF2-Rap1 complex has high specificity for telomeres and a higher affinity for 3Ј telomeric ends than hTRF2. Conclusion: hRap1 regulates the DNA binding characteristics of hTRF2. Significance: This is the first evidence of hRap1 interacting with DNA and altering the affinity of hTRF2 for telomeric DNA.

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Section: Discussionsupporting

confidence: 91%

Human Rap1 Interacts Directly with Telomeric DNA and Regulates TRF2 Localization at the Telomere

Arat

Griffith

2012

Journal of Biological Chemistry

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“…Of the later three steps of SSBR pathway, x-ray repair cross complementary 1 (XRCC1) is indispensible, because it not only acts as the scaffolding protein of SSBR, but also stimulates the activity of PNK (103). XRCC1 gene encoding protein (633 amino acids), consists of three functional domains -Nterminal domain (NTD), central breast cancer susceptibility protein-1 homology C-terminal (BRCT I), and C-terminal breast cancer susceptibility protein-1 homology C-terminal (BRCT II) (103)(104)(105)(106). This protein is directly associated with Pol β, DNA ligase III, and PARP, via their three functional domains and is implicated in the core processes in SSBR and BER pathway (103).…”

Section: Genetic Polymorphisms In Genes Involved In Ssbr Pathway and mentioning

confidence: 99%

DNA Repair Capacity-Related to Genetic Polymorphisms of DNA Repair Genes and Aflatoxin B1-Related Hepatocellular Carcinoma Among Chinese Population

Long¹,

Yao²,

Zeng³

et al. 2011

DNA Repair

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“…Although the significance of this interaction is not understood, a functional connection to DNA metabolism is preserved. To add to the complexity of the multiple interactions of XRCC1, it is known to bind single strand, nick, and gap DNA (24) and double strand DNA ends (25).…”

mentioning

confidence: 99%

Specificity of Protein Interactions Mediated by BRCT Domains of the XRCC1 DNA Repair Protein

Beernink

Hwang

Ramirez

et al. 2005

Journal of Biological Chemistry

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Protein interactions critical to DNA repair and cell cycle control systems are often coordinated by modules that belong to a superfamily of structurally conserved BRCT domains. Because the mechanisms of BRCT interactions and their significance are not well understood, we sought to define the affinity and specificity of those BRCT modules that orchestrate base excision repair and single-strand break repair. Common to these pathways is the essential XRCC1 DNA repair protein, which interacts with at least nine other proteins and DNA. Here, we characterized the interactions of four purified BRCT domains, two from XRCC1 and their two partners from DNA ligase III␣ and poly(ADP-ribosyl) polymerase 1. A monoclonal antibody was selected that recognizes the ligase III␣ BRCT domain, but not the other BRCT domains, and was used to capture the relevant ligase III␣ BRCT complex. To examine the assembly states of isolated BRCT domains and pairwise domain complexes, we used size-exclusion chromatography coupled with on-line light scattering. This analysis indicated that isolated BRCT domains form homo-oligomers and that the BRCT complex between the C-terminal XRCC1 domain and the ligase III␣ domain is a heterotetramer with 2:2 stoichiometry. Using affinity capture and surface plasmon resonance methods, we determined that specific heteromeric interactions with high nanomolar dissociation constants occur between pairs of cognate BRCT domains. A structural model for a XRCC1⅐DNA ligase III␣ heterotetramer is proposed as a core base excision repair complex, which constitutes a scaffold for higher order complexes to which other repair proteins and DNA are brought into proximity.

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The BRCT Regions of Tumor Suppressor BRCA1 and of XRCC1 Show DNA End Binding Activity with a Multimerizing Feature

Cited by 57 publications

References 27 publications

Human Rap1 Interacts Directly with Telomeric DNA and Regulates TRF2 Localization at the Telomere

Human Rap1 Interacts Directly with Telomeric DNA and Regulates TRF2 Localization at the Telomere

DNA Repair Capacity-Related to Genetic Polymorphisms of DNA Repair Genes and Aflatoxin B1-Related Hepatocellular Carcinoma Among Chinese Population

Specificity of Protein Interactions Mediated by BRCT Domains of the XRCC1 DNA Repair Protein

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