ICK(inhibitors of cyclin-dependent kinase)蛋白是细胞周期进程中关键的负调控因子。为解读禾本科作物ICK家族的蛋白功能及表达模式,本研究利用生物信息学方法对5种主要禾本科作物玉米、小麦、水稻、高粱、谷子进行全基因组扫描,分别...ICK(inhibitors of cyclin-dependent kinase)蛋白是细胞周期进程中关键的负调控因子。为解读禾本科作物ICK家族的蛋白功能及表达模式,本研究利用生物信息学方法对5种主要禾本科作物玉米、小麦、水稻、高粱、谷子进行全基因组扫描,分别鉴定到8、14、5、4、3个ICK家族成员,并对该基因家族特征、进化特点、蛋白结构等进行比对分析,通过已公布的转录组数据分析ICK基因在植株发育及逆境条件下的表达模式。结果表明:ICK家族成员C-末端均具有保守的ICK活性区,在进化树聚集为4个亚族,同一亚族之间拥有相似的基因结构及保守结构域分布。在进化过程中,ICK基因受到纯化选择,并拥有不同的进化轨迹。表达谱分析发现,ICK家族成员广泛响应不同非生物胁迫,具有时空表达特异性。研究结果可为ICK基因功能研究提供一定参考,并为禾本科作物抗逆育种提供靶向基因资源。展开更多
Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. Toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loop...Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. Toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loops 1–4, and C-terminal. Here, we used Mu-theraphotoxin-Ca2a(Ca2a), a peptide isolated from Cyriopagopus albostriatus, as a template to investigate the general properties of toxins in NaSpTx Family I. The toxins interacted with the cell membrane prior to binding to Nav1.7 via similar hydrophobic residues. Residues in loop 1, loop 4,and the C-terminal primarily interacted with the S3–S4 linker of domain II, especially basic amino acids binding to E818. We also identified the critical role of loop 2 in Ca2a regarding its affinity to Nav1.7.Our results provide further evidence that NaSpTx Family I toxins share similar structures and mechanisms of binding to Nav1.7.展开更多
文摘ICK(inhibitors of cyclin-dependent kinase)蛋白是细胞周期进程中关键的负调控因子。为解读禾本科作物ICK家族的蛋白功能及表达模式,本研究利用生物信息学方法对5种主要禾本科作物玉米、小麦、水稻、高粱、谷子进行全基因组扫描,分别鉴定到8、14、5、4、3个ICK家族成员,并对该基因家族特征、进化特点、蛋白结构等进行比对分析,通过已公布的转录组数据分析ICK基因在植株发育及逆境条件下的表达模式。结果表明:ICK家族成员C-末端均具有保守的ICK活性区,在进化树聚集为4个亚族,同一亚族之间拥有相似的基因结构及保守结构域分布。在进化过程中,ICK基因受到纯化选择,并拥有不同的进化轨迹。表达谱分析发现,ICK家族成员广泛响应不同非生物胁迫,具有时空表达特异性。研究结果可为ICK基因功能研究提供一定参考,并为禾本科作物抗逆育种提供靶向基因资源。
基金supported by the National Natural Science Foundation of China (31971190)Science Fund for Distinguished Young Scholars of Hunan Province (2021JJ10035)Education Department of Hunan Province (19A321)。
文摘Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. Toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loops 1–4, and C-terminal. Here, we used Mu-theraphotoxin-Ca2a(Ca2a), a peptide isolated from Cyriopagopus albostriatus, as a template to investigate the general properties of toxins in NaSpTx Family I. The toxins interacted with the cell membrane prior to binding to Nav1.7 via similar hydrophobic residues. Residues in loop 1, loop 4,and the C-terminal primarily interacted with the S3–S4 linker of domain II, especially basic amino acids binding to E818. We also identified the critical role of loop 2 in Ca2a regarding its affinity to Nav1.7.Our results provide further evidence that NaSpTx Family I toxins share similar structures and mechanisms of binding to Nav1.7.
