Caldas C, Kim M H, MacGregor A, Cain D, Aparicio S, Wiedemann L M
The Leukaemia Research Fund Centre at The Institute of Cancer Research, Chester Beatty Laboratories, London, UK.
Oncogene. 1998 Jun 25;16(25):3233-41. doi: 10.1038/sj.onc.1201873.
The MLL gene is interrupted and fused to a number of partner genes as a result of chromosomal translocations in human leukemias. MLL is a very large protein with a unique domain structure and large regions of homology to Drosophila trx. To define the key structural and functional domains of the MLL protein in vertebrates, we have cloned the genomic region encoding an MLL-like gene in the compact model vertebrate genome of Fugu rubripes. While the similarity between the mouse and human MLL proteins is very high, a lower overall similarity is present between the Fugu and mammalian proteins. Several new highly conserved regions were identified in the portion of the protein included in the MLL leukemia-associated fusion proteins. The conserved nature of regions of similarity between vertebrate forms of MLL and the Drosophila TRX proteins, as well as other domains previously suggested to have a functional role in MLL (including the AT hooks and the DNA methyltransferase domain), was also observed. Therefore, strong evolutionary constraints limited sequence divergence within these domains. The information derived from this comparative analysis will form the basis for the functional study of the MLL protein, particularly as it relates to human leukemogenesis.
在人类白血病中,由于染色体易位,MLL基因被中断并与许多伙伴基因融合。MLL是一种非常大的蛋白质,具有独特的结构域结构,并且在很大区域上与果蝇trx具有同源性。为了确定脊椎动物中MLL蛋白的关键结构和功能结构域,我们在红鳍东方鲀紧凑的模式脊椎动物基因组中克隆了编码MLL样基因的基因组区域。虽然小鼠和人类MLL蛋白之间的相似性非常高,但红鳍东方鲀和哺乳动物蛋白之间的总体相似性较低。在MLL白血病相关融合蛋白所含的蛋白质部分中鉴定出了几个新的高度保守区域。还观察到脊椎动物形式的MLL与果蝇TRX蛋白之间相似区域的保守性质,以及先前认为在MLL中具有功能作用的其他结构域(包括AT钩和DNA甲基转移酶结构域)。因此,强大的进化限制限制了这些结构域内的序列分歧。从这种比较分析中获得的信息将为MLL蛋白的功能研究奠定基础,特别是与人类白血病发生相关的研究。