循環型AMP依存型タンパク質キナーゼは,酵母転写活性化剤ADR1をリン酸化し,不活性化させます

J R Cherry¹, T R Johnson, C Dollard

¹Department of Biochemistry, University of New Hampshire, Durham 03824.

Cell

|February 10, 1989

まとめ

イーストの転写活性化活性化剤ADR1は,特定のキナーゼによってリン酸化され,このプロセスが遺伝子転写を調節することを示唆しています. ADR1に影響する変異

科学分野:

分子生物学は分子生物学である.
バイオケミストリーバイオケミストリー
イースト遺伝学イースト遺伝学

背景:

ユカリオットの遺伝子転写の調節には,しばしば転写因子のリン酸化が含まれます.
酵母におけるグルコース抑制の特殊なメカニズム,特にADH2遺伝子に関するものは,さらなる解明を必要としています.

研究の目的:

イーストの転写活性化剤ADR1.1.の調節におけるリン酸化の役割を調査する.
ADR1のリン酸化,ADH2の遺伝子発現,およびグルコース抑制の関係を決定する.

主な方法:

精製された酵母転写活性化剤ADR1と循環型AMP依存タンパク質キナーゼを用いたインビトロリン酸化アッセイ.
特定のADR1変異を有する酵母菌株におけるADR1酸化レベルの分析.
変化したキナーゼ活性がADH2発現に与える影響を評価するインビボ試験.

主要な成果:

イーストの転写活性化活性化剤ADR1は,サイクルAMP依存タンパク質キナーゼによってインビトロリン酸化される.
ADR1のADH2発現を活性化する能力を高める変異は,ADR1のリン酸化低下と相関しています.
活体内キナーゼ活性の増加は,ADR1アレル特異的な方法でADH2発現を抑制する.

結論:

ADH2遺伝子発現のグルコース抑制は,ADR1タンパク質のcAMP依存型リン酸化によって部分的に媒介されていることを示唆しています.
リン酸化はADR1調節タンパク質を無効化し,特定の条件下でADH2発現をダウンレギュレーションする.

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