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PHO80-PHO85细胞周期蛋白依赖性激酶复合物对PHO4核定位的调控。

Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex.

作者信息

O'Neill E M, Kaffman A, Jolly E R, O'Shea E K

机构信息

Department of Biochemistry and Biophysics, University of California at San Francisco, School of Medicine 94143-0448, USA.

出版信息

Science. 1996 Jan 12;271(5246):209-12. doi: 10.1126/science.271.5246.209.

Abstract

PHO4, a transcription factor required for induction of the PHO5 gene in response to phosphate starvation, is phosphorylated by the PHO80-PHO85 cyclin-CDK (cyclin-dependent kinase) complex when yeast are grown in phosphate-rich medium. PHO4 was shown to be concentrated in the nucleus when yeast were starved for phosphate and was predominantly cytoplasmic when yeast were grown in phosphate-rich medium. The sites of phosphorylation on PHO4 were identified, and phosphorylation was shown to be required for full repression of PHO5 transcription when yeast were grown in high phosphate. Thus, phosphorylation of PHO4 by PHO80-PHO85 turns off PHO5 transcription by regulating the nuclear localization of PHO4.

摘要

PHO4是一种转录因子,在酵母对磷酸盐饥饿作出反应时诱导PHO5基因表达所必需。当酵母在富含磷酸盐的培养基中生长时,PHO4会被PHO80-PHO85细胞周期蛋白依赖性激酶(CDK)复合物磷酸化。研究表明,当酵母缺乏磷酸盐时,PHO4集中在细胞核中;而当酵母在富含磷酸盐的培养基中生长时,PHO4主要存在于细胞质中。已确定PHO4的磷酸化位点,并且当酵母在高磷酸盐环境中生长时,磷酸化对于PHO5转录的完全抑制是必需的。因此,PHO80-PHO85对PHO4的磷酸化通过调节PHO4的核定位来关闭PHO5转录。

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