共查询到20条相似文献,搜索用时 30 毫秒
1.
2.
3.
4.
5.
Cys-3, the major sulfur regulatory gene of Neurospora crassa, encodes a regulatory protein that is capable of sequence-specific interaction with DNA. The interaction is mediated by a region within the CYS3 protein (the bzip region) which contains a potential dimer-forming surface, the leucine zipper, and an adjacent basic DNA contact region, NH2-terminal to the leucine zipper. To investigate the bipartite nature of the bzip region, a series of cys-3 mutants obtained by oligonucleotide-directed mutagenesis were expressed and tested for dimer formation as well as DNA binding and in vivo function. The results demonstrate that CYS3 protein exists as a dimer in the presence and absence of the target DNA and that dimerization of CYS3 is mediated strictly by the leucine zipper, which is required for both cys-3 function in vivo and DNA-binding activity in vitro. Furthermore, a truncated CYS3 protein corresponding to just the bzip region was found to mediate dimer formation and to possess DNA-binding activity. A CYS3 mutant protein with a pure methionine zipper showed significant, although reduced, function in vivo and in vitro. 相似文献
6.
7.
8.
9.
10.
11.
12.
13.
Thermal unfolding studies of a leucine zipper domain and its specific DNA complex: implications for scissor's grip recognition 总被引:11,自引:0,他引:11
M A Weiss 《Biochemistry》1990,29(35):8020-8024
14.
15.
16.
17.
18.
19.