MSH4 acts in conjunction with MLH1 during mammalian meiosis

التفاصيل البيبلوغرافية
العنوان: MSH4 acts in conjunction with MLH1 during mammalian meiosis
المؤلفون: Sabine Santucci-Darmanin, Françoise Lespinasse, Véronique Paquis-Flucklinger, Terry Ashley, Claude Desnuelle, Deepika Walpita
المساهمون: UMR 6549 CNRS, Centre National de la Recherche Scientifique (CNRS), Department of Genetics, Yale University School of Medecine, Department of Genetics, Yale University Scool of Medecine
المصدر: FASEB Journal
FASEB Journal, Federation of American Society of Experimental Biology, 2000, 14 (11), pp.1539-1547. ⟨10.1096/fj.99-0851com⟩
سنة النشر: 2000
مصطلحات موضوعية: Male, congenital, hereditary, and neonatal diseases and abnormalities, [SDV]Life Sciences [q-bio], Recombinant Fusion Proteins, Cell Cycle Proteins, MLH3, Biochemistry, Chromosomes, Chromosomal crossover, 03 medical and health sciences, Mice, 0302 clinical medicine, Adenosine Triphosphate, Spermatocytes, Genetics, Homologous chromosome, Animals, Humans, neoplasms, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Adaptor Proteins, Signal Transducing, Helix-Turn-Helix Motifs, Sequence Deletion, 0303 health sciences, Binding Sites, Chemistry, Synaptonemal Complex, Synapsis, Nuclear Proteins, DNA, Precipitin Tests, digestive system diseases, Neoplasm Proteins, Mice, Inbred C57BL, MSH5, Synaptonemal complex, Meiosis, MSH4, Homologous recombination, Carrier Proteins, MutL Protein Homolog 1, 030217 neurology & neurosurgery, Biotechnology, Protein Binding
الوصف: MSH4 is a meiosis-specific MutS homolog. In yeast, it is required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis I. MLH1 (MutL homolog 1) facilitates both mismatch repair and crossing over during meiosis in yeast. Germ-line mutations in the MLH1 human gene are responsible for hereditary nonpolyposis cancer, but the analysis of MLH1-deficient mice has revealed that MLH1 is also required for reciprocal recombination in mammals. Here we show that hMSH4 interacts with hMLH1. The two proteins are coimmunoprecipitated regardless of the presence of DNA or ATP, suggesting that the interaction does not require the binding of MSH4 to DNA. The domain of hMSH4 responsible for the interaction is in the amino-terminal part of the protein whereas the region that contains the ATP binding site and helix-turn-helix motif does not bind to hMLH1. Immunolocalization analysis shows that MSH4 is present at sites along the synaptonemal complex as soon as homologous chromosomes synapse. The number of MSH4 foci decreases gradually as pachynema progresses. During this transition, MLH1 foci begin to appear and colocalize with MSH4. These results suggest that MSH4 is first required for chromosome synapsis and that this MutS homologue is involved later with MLH1 in meiotic reciprocal recombination.
تدمد: 0892-6638
1530-6860
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::745daffca6c786413f75132221721a3dTest
https://pubmed.ncbi.nlm.nih.gov/10928988Test
حقوق: CLOSED
رقم الانضمام: edsair.doi.dedup.....745daffca6c786413f75132221721a3d
قاعدة البيانات: OpenAIRE