Steele S J, Levin H L
Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
J Virol. 1998 Nov;72(11):9318-22. doi: 10.1128/JVI.72.11.9318-9322.1998.
The yeast two-hybrid system and in vitro binding assays were used to characterize 54 potential interactions between the proteins of Tf1, an LTR-retrotransposon found in Schizosaccharomyces pombe. The Tf1 integrase (IN) protein was found to interact strongly with itself and not with other control proteins. In addition, the IN core domain interacted strongly with itself and full-length IN. Interestingly, the two-hybrid analysis detected an interaction between the RNase H domain of reverse transcriptase and IN. The biological implications of these interactions are discussed.
酵母双杂交系统和体外结合试验被用于表征粟酒裂殖酵母中发现的LTR反转录转座子Tf1的蛋白质之间的54种潜在相互作用。发现Tf1整合酶（IN）蛋白能与自身强烈相互作用，而不与其他对照蛋白相互作用。此外，IN核心结构域能与自身以及全长IN强烈相互作用。有趣的是，双杂交分析检测到逆转录酶的核糖核酸酶H结构域与IN之间存在相互作用。本文讨论了这些相互作用的生物学意义。
