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Gene Review:

RAD51AP1 - RAD51 associated protein 1

Homo sapiens

Synonyms: PIR51, RAD51-associated protein 1, RAD51-interacting protein

Henson, S.E. et al., Kovalenko, O.V. et al., Kovalenko, O.V. et al., Martinez, I. et al., Ohashi, A. et al., et al.

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Disease relevance of RAD51AP1

The Pir51 protein was expressed in Escherichia coli and purified to near homogeneity [1].
Fanconi anemia complementation group D2 (FANCD2) functions independently of BRCA2- and RAD51-associated homologous recombination in response to DNA damage [2].
Pir51, a Rad51-interacting protein with high expression in aggressive lymphoma, controls mitomycin C sensitivity and prevents chromosomal breaks [3].
Pir51, a protein of unknown function that interacts with Rad51, was identified in a screen for genes that were highly expressed in aggressive mantle cell lymphoma (MCL) versus indolent small lymphocytic lymphoma (SLL) patient samples [3].

High impact information on RAD51AP1

Our results suggest that FANCD2 mediates double strand DNA break repair independently of Rad51-associated homologous recombination [2].
During a search for Rad51-associated proteins in CHO nuclear extracts of S-phase cells by mass spectrometry of proteins immunoprecipitated with Rad51 antibodies, we identified a centrosomal protein, gamma-tubulin [4].
Pir51 mRNA is expressed in a number of human organs, most notably in testis, thymus, colon and small intestine [1].
The Pir51 protein may represent a new member of the multiprotein complexes postulated to carry out homologous recombination and DNA repair in mammalian cells [1].
The Pir51 gene locus was mapped to chromosome 12p13.1-13 [1].

Biological context of RAD51AP1

Analyses using truncations and point mutations in both RAD51AP1 and RAD51AP2 demonstrate that these proteins use the same structural motif for RAD51 binding [5].
We show that Pir51 is a nuclear protein expressed in a variety of cell types and that its expression is regulated during the cell cycle in a pattern nearly identical to Rad51 [3].
Yeast two-hybrid screening of a human testis cDNA library revealed a new protein, RAD51AP2 (RAD51 Associated Protein 2), that interacts strongly with RAD51 [5].

Physical interactions of RAD51AP1

RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51 [5].

Other interactions of RAD51AP1

The upregulated genes included those involved in cell cycle regulation (CDKN2A), cell differentiation (SFRP4) and DNA repair (RAD51AP1), while the downregulated genes included those involved in proteolysis (PRSS3) [6].
Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein [7].

References

A novel nucleic acid-binding protein that interacts with human rad51 recombinase. Kovalenko, O.V., Golub, E.I., Bray-Ward, P., Ward, D.C., Radding, C.M. Nucleic Acids Res. (1997) [Pubmed]
Fanconi anemia complementation group D2 (FANCD2) functions independently of BRCA2- and RAD51-associated homologous recombination in response to DNA damage. Ohashi, A., Zdzienicka, M.Z., Chen, J., Couch, F.J. J. Biol. Chem. (2005) [Pubmed]
Pir51, a Rad51-interacting protein with high expression in aggressive lymphoma, controls mitomycin C sensitivity and prevents chromosomal breaks. Henson, S.E., Tsai, S.C., Malone, C.S., Soghomonian, S.V., Ouyang, Y., Wall, R., Marahrens, Y., Teitell, M.A. Mutat. Res. (2006) [Pubmed]
DNA damage induce gamma-tubulin-RAD51 nuclear complexes in mammalian cells. Lesca, C., Germanier, M., Raynaud-Messina, B., Pichereaux, C., Etievant, C., Emond, S., Burlet-Schiltz, O., Monsarrat, B., Wright, M., Defais, M. Oncogene (2005) [Pubmed]
RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51. Kovalenko, O.V., Wiese, C., Schild, D. Nucleic Acids Res. (2006) [Pubmed]
Identification of differentially expressed genes in HPV-positive and HPV-negative oropharyngeal squamous cell carcinomas. Martinez, I., Wang, J., Hobson, K.F., Ferris, R.L., Khan, S.A. Eur. J. Cancer (2007) [Pubmed]
Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein. Li, W., Hesabi, B., Babbo, A., Pacione, C., Liu, J., Chen, D.J., Nickoloff, J.A., Shen, Z. Nucleic Acids Res. (2000) [Pubmed]

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