...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Plant Physiology and Biochemistry >Biochemical and phylogenetic analysis of CEBiP-like LysM domain-containing extracellular proteins in higher plants
【24h】

Biochemical and phylogenetic analysis of CEBiP-like LysM domain-containing extracellular proteins in higher plants

机译：高等植物中CEBiP样LysM结构域胞外蛋白的生化和系统发育分析

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

The chitin elicitor-binding protein (CEBiP) from rice was the first plant lysin motif (LysM) protein for which the biological and biochemical function had been established. It belongs to a plant-specific family of extracellular LysM proteins (LYMs) for which we analyzed the phylogeny. LYMs are present in vascular plants only, where an early gene duplication event might have resulted in two types which were retained in present day genomes. LYMs consist of a signal peptide, three consecutive LysMs, separated by cysteine pairs, and a C-terminal region without any known signature, whose length allows the distinction between the two types, and which may be followed by a glycosylphosphatidylinositol (GPI) anchor motif. We analyzed a representative of each type, MtLYM1 and MtLYM2, from Medicago truncatula at the biochemical level and with respect to their expression patterns and observed some similarities but also marked differences. MtLYM1 and MtLYM2 proved to be very different with regard to abundance and apparent molecular mass on SDS-PAGE. Both undergo several post-translational modifications, including N-glycosylation and the addition of a GPI anchor, which would position the proteins at the outer face of the plasma membrane. Only MtLYM2, but not MtLYM1, showed specific binding to biotinylated N-acetylchitooctaose in a manner similar to CEBiP, which belongs to the same type. We postulate that LYM2-type proteins likely function in the perception of chitin-related molecules, whereas possible functions of LYM1-type proteins remain to be elucidated.
机译：水稻的几丁质激发子结合蛋白（CEBiP）是第一个已确立其生物学和生化功能的植物溶素基序（LysM）蛋白。它属于植物特异的细胞外LysM蛋白（LYMs）家族，我们对其进行了系统进化分析。 LYM仅存在于维管植物中，早期的基因复制事件可能导致两种类型保留在当今的基因组中。 LYM由信号肽，被半胱氨酸对隔开的三个连续的LysM和一个C端区域组成，没有任何已知的特征，其长度允许区分两种类型，其后可以是糖基磷脂酰肌醇（GPI）锚定基序。我们在生化水平和表达方式方面分析了截叶苜蓿的每种类型的代表MtLYM1和MtLYM2，并观察到一些相似之处，但也有明显差异。在SDS-PAGE上，MtLYM1和MtLYM2在丰度和表观分子量方面有很大差异。两者都经历了几种翻译后修饰，包括N-糖基化和添加GPI锚，这会将蛋白质定位在质膜的外表面。仅MtLYM2，而不是MtLYM1，以与CEBiP相似的方式显示出与生物素化的N-乙酰壳聚糖八糖的特异性结合，属于同一类型。我们假设LYM2型蛋白可能在几丁质相关分子的感知中起作用，而LYM1型蛋白的可能功能尚待阐明。

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