Interaction between Auxin-binding Protein-I and RNA Polymerase II
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概要
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Interactions between auxin-binding protein-I (ABP-I), purified from etiolated mumg bean seedlings, and nuclear components from mung bean tissues were investigated. When NaCl-solubilized components of chromatin were put on an affinity column of ABP-I-linked Sepharose 4B, a small amount of the material was retained on the affinity column and was eluted with 1 M NaCl. RNA polymerase II activity was detected in the eluted fraction. Partially purified RNA polymerase II from mung bean nuclei and purified RNA polymerase II from wheat germ also bound to ABP-I. Indole-3-acetic acid was not necessary for the binding of RNA polymerase II to ABP-I. Acid-denatured ABP-I did not bind to RNA polymerase II from wheat germ. The addition of ABP-I to the reaction mixture for RNA synthesis in vitro caused a stimulation of the activity of wheat germ RNA polymerase.
- 社団法人日本農芸化学会の論文
- 1992-08-23
著者
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NAKAJIMA NOBUYOSHI
Institut fur Biotechnologie, Forschungszentrum Julich, Postfach 1913
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Kikuchi Motoyuki
Institute Of Biological Sciences University Of Tsukuba
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Sakai Shingo
Institute For Biochemical Regulation Faculty Of Agriculture Nagoya University
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Nakajima Nobuyoshi
Institute Of Biological Sciences University Of Tsukuba
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