• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Structural Environment Dictates the Biological Significance of Heme-Responsive Motifs and the Role of Hsp90 in the Activation of the Heme Activator Protein Hap1
【24h】

Structural Environment Dictates the Biological Significance of Heme-Responsive Motifs and the Role of Hsp90 in the Activation of the Heme Activator Protein Hap1

机译：结构环境决定了血红素响应性基序的生物学意义以及Hsp90在血红素激活蛋白Hap1激活中的作用。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Heme-responsive motifs (HRMs) mediate heme regulation of diverse regulatory proteins. The heme activator protein Hap1 contains seven HRMs, but only one of them, HRM7, is essential for heme activation of Hap1. To better understand the molecular basis underlying the biological significance of HRMs, we examined the effects of various mutations of HRM7 on Hap1. We found that diverse mutations of HRM7 significantly diminished the extent of Hap1 activation by heme and moderately enhanced the interaction of Hap1 with Hsp90. Furthermore, deletions of nonregulatory sequences completely abolished heme activation of Hap1 and greatly enhanced the interaction of Hap1 with Hsp90. These results show that the biological functions of HRMs and Hsp90 are highly sensitive to structural changes. The unique role of HRM7 in heme activation stems from its specific structural environment, not its mere presence. Likewise, the role of Hsp90 in Hap1 activation is dictated by the conformational or structural state of Hap1, not by the mere strength of Hap1-Hsp90 interaction. It appears likely that HRM7 and Hsp90 act together to promote the Hap1 conformational changes that are necessary for Hap1 activation. Such fundamental mechanisms of HRM-Hsp90 cooperation may operate in diverse regulatory systems to mediate signal transduction.
机译：血红素反应性基序（HRM）介导各种调节蛋白的血红素调节。血红素激活蛋白Hap1包含七个HRM，但是只有一个HRM7对Hap1的血红素激活至关重要。为了更好地理解HRM生物学意义的分子基础，我们检查了HRM7各种突变对Hap1的影响。我们发现HRM7的各种突变显着减少了血红素激活Hap1的程度，并适度增强了Hap1与Hsp90的相互作用。此外，删除非调控序列完全消除了Hap1的血红素激活，并大大增强了Hap1与Hsp90的相互作用。这些结果表明，HRM和Hsp90的生物学功能对结构变化高度敏感。 HRM7在血红素激活中的独特作用源于其特定的结构环境，而不仅仅是其存在。同样，Hsp90在Hap1激活中的作用由Hap1的构象或结构状态决定，而不是由Hap1-Hsp90相互作用的强度决定。 HRM7和Hsp90可能共同起作用，以促进Hap1激活所必需的Hap1构象变化。 HRM-Hsp90合作的这种基本机制可能在各种监管系统中发挥作用，以介导信号转导。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号