دورية أكاديمية
Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination.
العنوان: | Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination. |
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المؤلفون: | Wiese C; Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. cwiese@lbl.gov, Hinz JM, Tebbs RS, Nham PB, Urbin SS, Collins DW, Thompson LH, Schild D |
المصدر: | Nucleic acids research [Nucleic Acids Res] 2006 May 22; Vol. 34 (9), pp. 2833-43. Date of Electronic Publication: 2006 May 22 (Print Publication: 2006). |
نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
اللغة: | English |
بيانات الدورية: | Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Electronic-Print Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE |
أسماء مطبوعة: | Publication: 1992- : Oxford : Oxford University Press Original Publication: London, Information Retrieval ltd. |
مواضيع طبية MeSH: | Recombination, Genetic*, Adenosine Triphosphatases/*chemistry , DNA-Binding Proteins/*chemistry, Amino Acid Motifs ; Amino Acid Sequence ; Animals ; CHO Cells ; Cricetinae ; Cricetulus ; DNA Damage ; DNA Repair ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Genetic Complementation Test ; Humans ; Immunoprecipitation ; Molecular Sequence Data ; Mutation ; Rad51 Recombinase/metabolism ; Two-Hybrid System Techniques |
مستخلص: | In vertebrates, homologous recombinational repair (HRR) requires RAD51 and five RAD51 paralogs (XRCC2, XRCC3, RAD51B, RAD51C and RAD51D) that all contain conserved Walker A and B ATPase motifs. In human RAD51D we examined the requirement for these motifs in interactions with XRCC2 and RAD51C, and for survival of cells in response to DNA interstrand crosslinks (ICLs). Ectopic expression of wild-type human RAD51D or mutants having a non-functional A or B motif was used to test for complementation of a rad51d knockout hamster CHO cell line. Although A-motif mutants complement very efficiently, B-motif mutants do not. Consistent with these results, experiments using the yeast two- and three-hybrid systems show that the interactions between RAD51D and its XRCC2 and RAD51C partners also require a functional RAD51D B motif, but not motif A. Similarly, hamster Xrcc2 is unable to bind to the non-complementing human RAD51D B-motif mutants in co-immunoprecipitation assays. We conclude that a functional Walker B motif, but not A motif, is necessary for RAD51D's interactions with other paralogs and for efficient HRR. We present a model in which ATPase sites are formed in a bipartite manner between RAD51D and other RAD51 paralogs. |
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معلومات مُعتمدة: | CA112566 United States CA NCI NIH HHS; R01 CA112566 United States CA NCI NIH HHS; CA89405 United States CA NCI NIH HHS; P01 CA092584 United States CA NCI NIH HHS; P01 CA92584 United States CA NCI NIH HHS; R01 CA089405 United States CA NCI NIH HHS |
المشرفين على المادة: | 0 (DNA-Binding Proteins) 0 (RAD51D protein, human) EC 2.7.7.- (Rad51 Recombinase) EC 3.6.1.- (Adenosine Triphosphatases) |
تواريخ الأحداث: | Date Created: 20060524 Date Completed: 20060607 Latest Revision: 20181113 |
رمز التحديث: | 20240628 |
مُعرف محوري في PubMed: | PMC1464408 |
DOI: | 10.1093/nar/gkl366 |
PMID: | 16717288 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1362-4962 |
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DOI: | 10.1093/nar/gkl366 |