THE 4 HUMAN MUSCLE REGULATORY HELIX-LOOP-HELIX PROTEINS MYF3-MYF6 EXHIBIT SIMILAR HETERO-DIMERIZATION AND DNA-BINDING PROPERTIES
THE 4 HUMAN MUSCLE REGULATORY HELIX-LOOP-HELIX PROTEINS MYF3-MYF6 EXHIBIT SIMILAR HETERO-DIMERIZATION AND DNA-BINDING PROPERTIES
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DOI：
10.1093/nar/19.20.5645
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发表时间：
1991-10-25
影响因子：
14.9
通讯作者：
ARNOLD, HH
中科院分区：
文献类型：
--
作者：
BRAUN, T;ARNOLD, HH
肌肉调节蛋白Myf 3、Myf 4、Myf 5和Myf 6共享由碱性氨基酸簇和潜在的螺旋-环-螺旋结构组成的高度保守的DNA结合和二聚化结构域。在这里，我们证明了四种人类肌肉特异性HLH蛋白具有相似的DNA结合和二聚化特性。该家族的成员与普遍表达的HLH蛋白E12、E2-2和E2-5形成具有可比稳定性的蛋白质复合物，并在体外以相似的效率结合命名为E-box的保守DNA序列CANNTG。各种复合物的结合亲和力受到共有基序的可变内部和侧翼核苷酸的极大影响。Myf蛋白彼此组合以及与来自人T细胞的HLH蛋白lyl-1的组合在体外不与DNA结合。我们的研究结果表明，各种组织特异性和更广泛表达的HLH因子的组合协会不会导致DNA序列的Myf蛋白的差异识别。
The muscle regulatory proteins Myf3, Myf4, Myf5, and Myf6 share a highly conserved DNA binding and dimerization domain consisting of a cluster of basic amino acids and a potential helix-loop-helix structure. Here we demonstrate that the four human muscle-specific HLH proteins have similar DNA binding and dimerization properties. The members of this family form protein complexes of comparable stability with the ubiquitously expressed HLH proteins E12, E2-2, and E2-5 and bind to the conserved DNA sequence CANNTG designated as E-box with similar efficiency in vitro. The binding affinities of the various complexes are greatly influenced by the variable internal and flanking nucleotides of the consensus motif. Combinations of Myf proteins with one another and with lyl-1, an HLH protein from human T cells, do not bind to DNA in vitro. Our results suggest that combinatorial associations of the various tissue-specific and more widely expressed HLH factors do not result in differential recognition of DNA sequences by Myf proteins.