PHOSPHORYLATION OF INITIATION FACTOR-2-ALPHA BY PROTEIN-KINASE GCN2 MEDIATES GENE-SPECIFIC TRANSLATIONAL CONTROL OF GCN4 IN YEAST

被引：664

作者：

DEVER, TE ^{[1
]}

FENG, L ^{[1
]}

WEK, RC ^{[1
]}

CIGAN, AM ^{[1
]}

DONAHUE, TF ^{[1
]}

HINNEBUSCH, AG ^{[1
]}

机构：

[1] INDIANA UNIV, DEPT BIOL, BLOOMINGTON, IN 47405 USA

来源：

CELL | 1992年 / 68卷 / 03期

关键词：

D O I：

10.1016/0092-8674(92)90193-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

We show that phosphorylation of the a subunit of eukaryotic translation initiation factor 2 (eIF-2) by the protein kinase GCN2 mediates translational control of the yeast transcriptional activator GCN4. In vitro, GCN2 specifically phosphorylates the alpha-subunit of rabbit or yeast eIF-2. In vivo, phosphorylation of eIF-2-alpha increases in response to amino acid starvation, which is dependent on GCN2. Substitution of Ser-51 with alanine eliminates phosphorylation of eIF-2-alpha by GCN2 in vivo and in vitro and abolishes increased expression of GCN4 and amino acid biosynthetic genes under its control in amino acid-starved cells. The Asp-51 substitution mimics the phosphorylated state and derepresses GCN4 in the absence of GCN2. Thus, an established mechanism for regulating total protein synthesis in mammalian cells mediates gene-specific translational control in yeast.

引用

页码：585 / 596

页数：12

共 47 条

[1]

SUPPRESSION OF RIBOSOMAL REINITIATION AT UPSTREAM OPEN READING FRAMES IN AMINO ACID-STARVED CELLS FORMS THE BASIS FOR GCN4 TRANSLATIONAL CONTROL [J].