GAL4 IS PHOSPHORYLATED AS A CONSEQUENCE OF TRANSCRIPTIONAL ACTIVATION

被引：63

作者：

SADOWSKI, I ^{[1
]}

NIEDBALA, D ^{[1
]}

WOOD, K ^{[1
]}

PTASHNE, M ^{[1
]}

机构：

[1] HARVARD UNIV, DEPT BIOCHEM & MOLEC BIOL, CAMBRIDGE, MA 02138 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 23期

关键词：

YEAST ACTIVATORS; GAL4; MUTANTS; PROTEIN KINASES;

D O I：

10.1073/pnas.88.23.10510

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

GAL4 protein isolated from yeast in which it is active is phosphorylated predominantly on two different serine residues. One of these was identified as Ser-837; substitution of this residue for alanine has no detectable effect on transcriptional activation by GAL4. Phosphorylation at Ser-837 requires that both the DNA binding and transcriptional activation functions be intact. We propose that some phosphorylations of GAL4, including that at Ser-837, occur concomitantly with activation of transcription.

引用

页码：10510 / 10514

页数：5

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