...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >EVIDENCE THAT THE 50-KDA SUBSTRATE OF BREFELDIN A-DEPENDENT ADP-RIBOSYLATION BINDS GTP AND IS MODULATED BY THE G-PROTEIN BETA-GAMMA SUBUNIT COMPLEX
【24h】

EVIDENCE THAT THE 50-KDA SUBSTRATE OF BREFELDIN A-DEPENDENT ADP-RIBOSYLATION BINDS GTP AND IS MODULATED BY THE G-PROTEIN BETA-GAMMA SUBUNIT COMPLEX

机译：证据表明，视黄素A依赖性的ADP-核糖基化的50-KDA底物与GTP结合并由G蛋白β-γ亚基复合物调节

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Brefeldin A, a fungal metabolite that inhibits membrane transport, induces the mono(ADP-ribosyl)ation of two cytosolic proteins of 38 and 50 kDa as judged by SDS/PAGE. The 38-kDa substrate has been previously identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). We report that the 50-kDa BFA-induced ADP-ribosylated substrate (BARS-50) has native forms of 170 and 130 kDa, as determined by gel filtration of rat brain cytosol, indicating that BARS-50 might exist as a multimeric complex. BARS-50 can bind GTP, as indicated by blot-overlay studies with [alpha-P-32]GTP and by photoaffinity labeling with guanosine 5'-[gamma-P-32][beta,gamma-(4-azidoanilido)] triphosphate. Moreover, ADP-ribosylation of BARS-50 was completely inhibited by the beta gamma subunit complex of G proteins, while the ADP-ribosylation of GAPDH was unmodified, indicating that this effect was due to an interaction of the py complex with BARS-50, rather than with the ADP-ribosylating enzyme. Two-dimensional gel electrophoresis and immunoblot analysis shows that BARS-50 is a group of closely related proteins that appear to be different from all the known GTP-binding proteins. [References: 34]
机译：布雷菲德菌素A是一种抑制膜运输的真菌代谢产物，可诱导SDS / PAGE判断两个38 kDa和50 kDa胞质蛋白的单（ADP-核糖基）化。 38 kDa的底物先前已被确定为3-磷酸甘油醛脱氢酶（GAPDH）。我们报道50-kDa BFA诱导的ADP-核糖基化底物（BARS-50）具有170和130 kDa的天然形式，这是通过大鼠脑细胞溶质的凝胶过滤确定的，表明BARS-50可能以多聚体形式存在。 BARS-50可以结合GTP，如用[α-P-32] GTP进行的印​​迹叠加研究以及用鸟苷5'-[γ-P-32]β，γ-（4-叠氮基安利多）进行光亲和标记所表明的那样三磷酸。此外，G蛋白的βγ亚基复合物完全抑制了BARS-50的ADP-核糖基化，而GAPDH的ADP-核糖基化未修饰，表明该作用是由于py复合物与BARS-50的相互作用所致，而不是使用ADP-核糖基化酶。二维凝胶电泳和免疫印迹分析表明，BARS-50是一组紧密相关的蛋白，似乎与所有已知的GTP结合蛋白都不同。 [参考：34]

著录项

相似文献

  • 外文文献
  • 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