MSG5, A NOVEL PROTEIN PHOSPHATASE PROMOTES ADAPTATION TO PHEROMONE RESPONSE IN SACCHAROMYCES-CEREVISIAE

MSG5, A NOVEL PROTEIN PHOSPHATASE PROMOTES ADAPTATION TO PHEROMONE RESPONSE IN SACCHAROMYCES-CEREVISIAE
复制标题

DOI:
10.1002/j.1460-2075.1994.tb06235.x
复制
发表时间:
1994-01-01
期刊:
影响因子:
11.4
通讯作者:
MATSUMOTO, K
MATSUMOTO, K
中科院分区:
生物学1区
文献类型:
--
作者:
DOI, K;GARTNER, A;MATSUMOTO, K

文献摘要

被引文献

相似文献

信息素刺激的酵母细胞和单倍体 gpa1 缺失突变体将其细胞周期停滞在 G(1) 中。一种称为 MSG5 的新基因的过度表达会抑制这种细胞分裂的抑制。 MSG5 功能的丧失会导致对信息素的适应性反应减弱。遗传分析表明,MSG5 在蛋白激酶 STE7 和 FUS3 发挥作用以传递信息素诱导信号的阶段发挥作用。由于 MSG5 功能的丧失会导致 FUS3 酶活性增加,但不会导致 STE7 活性增加,因此我们认为 MSG5 会影响 FUS3 的通路。序列分析表明 MSG5 编码蛋白质酪氨酸磷酸酶。重组 MSG5 在体外具有磷酸酶活性并且能够灭活自磷酸化 FUS3 的发现支持了这一点。因此,MSG5 可能通过调节 FUS3 的磷酸化状态来刺激信息素的恢复。
Pheromone-stimulated yeast cells and haploid gpa1 deletion mutants arrest their cell cycle in G(1). Overexpression of a novel gene called MSG5 suppresses this inhibition of cell division. Loss of MSG5 function leads to a diminished adaptive response to pheromone. Genetic analysis indicates that MSG5 acts at a stage where the protein kinases STE7 and FUS3 function to transmit the pheromone-induced signal. Since loss of MSG5 function causes an increase in FUS3 enzyme activity but not STE7 activity, we propose that MSG5 impinges on the pathway at FUS3. Sequence analysis suggests that MSG5 encodes a protein tyrosine phosphatase. This is supported by the finding that recombinant MSG5 has phosphatase activity in vitro and is able to inactivate autophosphorylated FUS3. Thus MSG5 might stimulate recovery from pheromone by regulating the phosphorylation state of FUS3.