作者: Hui Yang , Tianlong Zhang , Ye Tao , Lijing Wu , Hong-tao Li
DOI: 10.1016/J.STR.2011.12.012
关键词:
摘要: Fanconi anemia (FA) is a chromosomal instability disorder associated with deficiencies in the complementation group (FANC) network. A complex consisting of FANCM-associated histone-fold proteins 1 and 2 (MHF1 MHF2) has been shown to act cooperatively FANCM DNA damage repair FA pathway. Here we report structure Saccharomyces cerevisiae MHF which MHF1 MHF2 assume typical histone fold, heterotetrameric architecture similar that histones (H3-H4)₂ heterotetramer. Loop L2 probably involved binding, loop L3 helices α2 α3 one subunit interact those other form two heterotetramer interfaces. Further genetic data demonstrate assembly essential for function repair. These results provide, best our knowledge, new mechanistic insights into complex.