Interaction between the helicase domain of the tobacco mosaic virus replicase and a tobacco arginine decarboxylase

被引：5
|
作者：
Shimizu T. [1 ,2 ]
Yamaji Y. [1 ]
Ogasawara Y. [1 ]
Hamada K. [1 ]
Sakurai K. [1 ]
Kobayashi T. [1 ]
Watanabe T. [1 ]
Hibi T. [1 ]
机构：
[1] Laboratory of Plant Pathology, Grad. Sch. of Agric. and Life Sci., University of Tokyo, Bunkyo-ku, Tokyo 113-8657
[2] Natl. Agricultural Research Center, Ibaraki
来源：
Journal of General Plant Pathology | 2004年 / 70卷 / 6期
基金：
日本学术振兴会;
关键词：
Arginine decarboxylase; Nicotiana tabacum; Replicase; Tobacco mosaic virus; Yeast two-hybrid screening;
D O I：
10.1007/s10327-004-0139-2
中图分类号：
学科分类号：
摘要：
In a yeast two-hybrid screening test for tobacco proteins that interact with TMV replicase using the helicase (H) domain as bait, a cDNA clone was selected that encodes a polyamine biosynthetic enzyme, arginine decarboxylase (ADC). In yeast cells, the C-terminal internal region of ADC interacted with the H domain. This observation was confirmed in vitro by far-Western blotting. Inhibition of the binding between the H domain and the IRnHEL (I region and N-terminus of helicase domain) region by ADC using a yeast three-hybrid assay suggested possible interference of the heterodimerization of 126K and 183K by ADC.
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页码：353 / 358
页数：5
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