Protein-protein interactions mapped by artificial proteases:: where σ factors bind to RNA polymerase

被引:42
作者
Datwyler, SA [1 ]
Meares, CF [1 ]
机构
[1] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA
关键词
D O I
10.1016/S0968-0004(00)01652-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Interactions between proteins are important to understand but difficult to study. Conjugating a protein to a small artificial protease endows it with the ability to cut other proteins where it binds to them. Analysing the sites cut on the target proteins leads to new understanding of the structure of each complex. The binding of a factors to a common region on RNA polymerase provides an example.
引用
收藏
页码:408 / 414
页数:7
相关论文
共 44 条
  • [41] TULLIUS TD, 1987, METHOD ENZYMOL, V155, P537
  • [42] Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes
    Wigneshweraraj, SR
    Fujita, N
    Ishihama, A
    Buck, M
    [J]. EMBO JOURNAL, 2000, 19 (12) : 3038 - 3048
  • [43] RNA POLYMERASE-II
    YOUNG, RA
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1991, 60 : 689 - 715
  • [44] Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    Zhang, GY
    Campbell, EA
    Minakhin, L
    Richter, C
    Severinov, K
    Darst, SA
    [J]. CELL, 1999, 98 (06) : 811 - 824