...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of bacteriology >Purification and Characterization of a Hemolysin-Like Protein, Sll1951, a Nontoxic Member of the RTX Protein Family from the Cyanobacterium Synechocystis sp. Strain PCC 6803
【24h】

Purification and Characterization of a Hemolysin-Like Protein, Sll1951, a Nontoxic Member of the RTX Protein Family from the Cyanobacterium Synechocystis sp. Strain PCC 6803

机译：溶血素样蛋白Sll1951的纯化和表征，该蛋白来自蓝藻蓝藻属RTX蛋白家族的无毒成员。应变PCC 6803

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

摘要

The hemolysin-like protein (HLP) Sll1951, characterized by the GGXGXDXUX nonapeptide motif implicated in Ca2+ binding, was purified from the glucose-tolerant strain (GT) of Synechocystis sp. strain PCC 6803. HLP was eluted at 560 kDa after gel filtration chromatography. Atomic absorption spectroscopy indicated that the protein bound calcium. The bound Ca2+ was not chelated with EGTA; however, it was released after being heated at 100°C for 1 min, and it rebound to the Ca2+-depleted protein at room temperature. The apparent HLP molecular mass increased to 1,000 kDa and reverted to 560 kDa during the release and rebinding of Ca2+, respectively. The monomers of the respective forms appeared at 90 and 200 kDa after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. HLP showed no apparent hemolytic activity against sheep erythrocytes; however, a slight hemolytic activity was detected during the conformational change caused by the rebinding of Ca2+. Immunoelectron microscopy using polyclonal antibodies against the 200-kDa monomer revealed that HLP is located in the cell surface layer. The localization and Ca2+-induced reversible conformational change suggest that HLP is a member of the repeat in toxin (RTX) protein family despite its latent and low toxicity. In some other cyanobacteria, RTX proteins are reported to be necessary for cell motility. However, the GT was immotile. Moreover, the motile wild-type strain did not express any HLP, suggesting that HLP is one of the factors involved in the elimination of motility in the GT. We concluded that the involvement of RTX protein in cyanobacterial cell motility is not a general feature.
机译：从溶血性囊藻的耐葡萄糖菌株（GT）中纯化出溶血素样蛋白（HLP）Sll1951，其特征在于与Ca 2 + 结合的GGXGXDXUX非肽基序。 sp。菌株PCC6803。在凝胶过滤层析后以560kDa洗脱HLP。原子吸收光谱法表明该蛋白质结合了钙。结合的Ca 2 + 未与EGTA螯合;然而，它在100°C加热1分钟后被释放，并在室温下反弹至贫化了Ca 2 + 的蛋白质。在Ca 2 + 的释放和重新结合过程中，表观HLP分子量分别增加到1,000 kDa和恢复到560 kDa。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后，相应形式的单体出现在90和200 kDa处。 HLP对羊红细胞没有明显的溶血活性。然而，由于Ca 2 + 的重新结合而引起的构象变化期间，检测到轻微的溶血活性。使用针对200 kDa单体的多克隆抗体进行的免疫电子显微镜检查显示，HLP位于细胞表面层。本地化和Ca 2 + 诱导的可逆构象变化表明，尽管HLP具有潜在性和低毒性，但它是毒素（RTX）蛋白家族重复序列的成员。在其他一些蓝细菌中，据报道RTX蛋白是细胞运动所必需的。但是，GT的动力不足。而且，运动型野生型菌株不表达任何HLP，这表明HLP是参与GT运动性消除的因素之一。我们得出的结论是，RTX蛋白与蓝细菌细胞运动无关。

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