Research on the RNA polymerase which has an affinity for auxin-binding protein.
| Project/Area Number |
62480008
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
植物生理学
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| Research Institution | Saitama University |
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Principal Investigator |
SAKAI Shingo Faculty of Science,Saitama University Associate Professor, 理学部, 助教授 (60033388)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥6,200,000 (Direct Cost: ¥6,200,000)
Fiscal Year 1988: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1987: ¥5,200,000 (Direct Cost: ¥5,200,000)
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| Keywords | Auxin-binding protein / Gene expression / RNAポリメラーゼII / RNAポリメラーゼ |
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| Research Abstract |
Nucleoproteins were solubilized from isolated mung bean nuclei and separated by a column of mono Q. Fractions of alpha-amanitin-sensitive RNA polymerase activity were pooled and applied to a column of auxin-binding protein-I(ABP-I)-bound Sepharose 4B. RNA polymerase activity was completely retained on the column and eluted by 0.3 M (NH_4)@>D22@>D2SO_4.
RNA polymerase II was purified from wheat germ by the method of Burgess et al. and examined an interaction for ABP-I. The purified TNA polymerase II was retained on the affinity column of ABP-I-bound Sepharose 4B and eluted by 0.3 M (NH_4)_2SO_4.
From these results, we consider that RNA polymerase II have an affinity for ABP-I and the interaction may play a role for gene expression.
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Report
(3 results)
Research Products
(7 results)
