Identification of a Novel HumanRAD51Homolog,RAD51B

Albala, Joanna S.; Thelen, Michael P.; Prange, Christa; Fan, Wufang; Christensen, Mari; Thompson, Larry H.; Lennon, Gregory G.

doi:10.1006/geno.1997.5062

Cited by 115 publications

(55 citation statements)

References 28 publications

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“…The proteins maintained at an elevated level in the radiation-derived MCF-7 cells are correlated to cell cycle control, apoptosis, DNA repair, and cell proliferation. The genes responsible for this elevation include: RAD51B, which encodes a DNA repair protein RAD51 homolog 2, which is involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents (28). CCNH encodes cyclin H, which regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex.…”

Section: Discussionmentioning

confidence: 99%

Protein expression pattern in response to ionizing radiation in MCF-7 human breast cancer cells

Jung

Lee

et al. 2011

Oncology Letters

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Abstract. Breast cancer is one of the most common types of cancer in women and is highly treatable by radiotherapy. However, repeated exposure to radiation results in tumor cell resistance. Understanding the molecular mechanisms involved in the response of tumors to γ-irradiation is important for improving radiotherapy. For this reason, we aimed to identify radiation-responsive genes at the protein level. In the present study, we observed differentially expressed proteins using 2D-PAGE and MALDI-TOF-MS for the global analysis of protein expression patterns in response to ionizing radiation (IR). When the expression patterns of proteins were compared to a control gel, numerous spots were found that differed greatly. Among them, 11 spots were found to be significantly different. One set of proteins (GH2, RGS17, BAK1, CCNH, TSG6, RAD51B, IGFBP1 and CASP14) was upregulated and another set of proteins (C1QRF, PLSCR2 and p34 SE1-1 ) was downregulated after exposure to γ-rays. These proteins are known to be related to cell cycle control, apoptosis, DNA repair, cell proliferation and other signaling pathways.

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Section: Discussionmentioning

confidence: 99%

Protein expression pattern in response to ionizing radiation in MCF-7 human breast cancer cells

Jung

Lee

et al. 2011

Oncology Letters

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“…Five paralogs of human RAD51 have been identified: RAD51B (hREC2, RAD51L1), RAD51C (RAD51L2), RAD51D (RAD51L3), XRCC2, and XRCC3; these proteins share ϳ25% amino acid sequence identity with one another and RAD51 (5)(6)(7)(8)(9). DT40 chicken cell knockouts have been generated for each paralog, all of which exhibit a lack of RAD51 foci formation as well as enhanced radiation and cisplatin sensitivity, consistent with a deficiency in recombinational repair (10,11).…”

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confidence: 87%

RAD51C Interacts with RAD51B and Is Central to a Larger Protein Complex in Vivo Exclusive of RAD51

Miller¹,

Yoshikawa²,

McConnell³

et al. 2002

Journal of Biological Chemistry

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RAD51B and RAD51C are two of five known paralogs of the human RAD51 protein that are thought to function in both homologous recombination and DNA double-strand break repair. This work describes the in vitro and in vivo identification of the RAD51B/RAD51C heterocomplex. The RAD51B/RAD51C heterocomplex was isolated and purified by immunoaffinity chromatography from insect cells co-expressing the recombinant proteins. Moreover, co-immunoprecipitation of the RAD51B and RAD51C proteins from HeLa, MCF10A, and MCF7 cells strongly suggests the existence of an endogenous RAD51B/RAD51C heterocomplex. We extended these observations to examine the interaction between the RAD51B/RAD51C complex and the other RAD51 paralogs. Immunoprecipitation using protein-specific antibodies showed that RAD51C is central to a single large protein complex and/or several smaller complexes with RAD51B, RAD51D, XRCC2, and XRCC3. However, our experiments showed no evidence for the inclusion of RAD51 within these complexes. Further analysis is required to elucidate the function of the RAD51B/RAD51C heterocomplex and its association with the other RAD51 paralogs in the processes of homologous recombination and DNA double-strand break repair.The human RAD51 protein functions in homologous recombination and DNA double-strand break repair (1-4). Five paralogs of human RAD51 have been identified: RAD51B (hREC2, RAD51L1), RAD51C (RAD51L2), RAD51D (RAD51L3), XRCC2, and XRCC3; these proteins share ϳ25% amino acid sequence identity with one another and RAD51 (5-9). DT40 chicken cell knockouts have been generated for each paralog, all of which exhibit a lack of RAD51 foci formation as well as enhanced radiation and cisplatin sensitivity, consistent with a deficiency in recombinational repair (10, 11). These results are consistent with previous work, which showed that the XRCC3 knockout CHO cell line (irs1SF) is deficient in RAD51 foci formation, suggesting that XRCC3 is required for RAD51 function (12). Similarly, XRCC2-defective cell lines also fail to form damage-dependent RAD51 foci (13). Furthermore, both XRCC2 and XRCC3 have been shown to be required for repair of double-strand breaks by homologous recombination in vivo (14 -16). Initially by sequence and now by association and function, it has become increasingly evident that these RAD51 paralogs participate together in recombination and repair processes.Extensive yeast two-and three-hybrid analysis suggests that there are a variety of putative protein-protein interactions between the RAD51 paralogs. These include XRCC2/RAD51D (17, 18) and XRCC3/RAD51(19). Moreover, interactions have been suggested between RAD51C/RAD51B, RAD51C/RAD51D, RAD51C/XRCC3, and RAD51C/RAD51 (8, 18). More recent biochemical evidence has corroborated the interaction between XRCC2 and RAD51D by co-purification of the recombinant proteins and co-elution of the native proteins by gel filtration from mammalian cell extracts; RAD51D was further shown to be a DNA-stimulated ATPase (17). In addition, a stable heterocomplex was demons...

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“…Evidence has also been presented that RAD51L1 (formerly RAD51B), a member of the RAD51 recombination repair gene family (Albala et al 1997;Shinohara et al 1992), is the chromosome 14 target gene and preferential fusion partner of HMGIC in uterine leiomyomas with t(12;14) (Amant et al 2001;Ingraham et al 1999;Schoenmakers et al 1999;Takahashi et al 2001). Although the RAD51L1 protein has not yet been shown to catalyze recombination reactions, RAD51L1 appears to be an essential gene (Shu et al 1999) expressed in almost all organs and tissues (Rice et al 1997) and probably plays a role in regulation of cell cycle progression (Havre et al 1998(Havre et al , 2000.…”

Section: The Genetic Findingsmentioning

confidence: 99%

Etiology and pathogenesis of uterine leiomyomas: a review.

Flake

Andersen

Dixon

2003

Environ Health Perspect

497

392

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Uterine leiomyomas, or fibroids, represent a major public health problem. It is believed that these tumors develop in the majority of American women and become symptomatic in one-third of these women. They are the most frequent indication for hysterectomy in the United States. Although the initiator or initiators of fibroids are unknown, several predisposing factors have been identified, including age (late reproductive years), African-American ethnicity, nulliparity, and obesity. Nonrandom cytogenetic abnormalities have been found in about 40% of tumors examined. Estrogen and progesterone are recognized as promoters of tumor growth, and the potential role of environmental estrogens has only recently been explored. Growth factors with mitogenic activity, such as transforming growth factor-β 3, basic fibroblast growth factor, epidermal growth factor, and insulin-like growth factor-I, are elevated in fibroids and may be the effectors of estrogen and progesterone promotion. These data offer clues to the etiology and pathogenesis of this common condition, which we have analyzed and summarized in this review.

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Identification of a Novel HumanRAD51Homolog,RAD51B

Cited by 115 publications

References 28 publications

Protein expression pattern in response to ionizing radiation in MCF-7 human breast cancer cells

Protein expression pattern in response to ionizing radiation in MCF-7 human breast cancer cells

RAD51C Interacts with RAD51B and Is Central to a Larger Protein Complex in Vivo Exclusive of RAD51

Etiology and pathogenesis of uterine leiomyomas: a review.

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