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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-12

AUTHORS

Takumi Shimizu, Yasuyuki Yamaji, Yoshitake Ogasawara, Koji Hamada, Keitaro Sakurai, Toshihiko Kobayashi, Takato Watanabe, Tadaaki Hibi

ABSTRACT

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 126 K and 183 K by ADC. More... »

PAGES

353-358

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10327-004-0139-2

DOI

http://dx.doi.org/10.1007/s10327-004-0139-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048556404


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