Structural basis for the specific single-stranded RNA recognition by designer pentatricopeptide repeat protein
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- 英文论文题名：Structural basis for the specific single-stranded RNA recognition by designer pentatricopeptide repeat protein
- 论文作者：Ping Yin
- 英文论文作者：Ping Yin ; National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research
- 年：2016
- 作者机构：National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research;
- 会议召开时间：2016-04-27
- 会议录名称：第五届中国结构生物学学术讨论会摘要集
- 语种：英文
- 分类号：Q78
- 学会代码：ZGWI
- 会议名称：第五届中国结构生物学学术讨论会
- 会议地点：中国广东深圳
- 主办单位：中国生物物理学会分子生物物理学专业委员会
- 学会名称：中国生物物理学会
- 页数：1
- 文件大小：144k
- 原文格式：D
- 会议级别：全国
摘要
As a large family of RNA binding proteins, pentatricopeptide repeat(PPR) proteins mediate multiple aspects of RNA metabolism in eukaryotes. Binding to their target single-stranded RNA(ss RNA) in a modular and base-specific fashion, PPR proteins can serve as designable modules for gene manipulation. However, the structural basis for nucleotide-specific recognition by designer PPR(d PPR) remains to be elucidated. Here we report four crystal structures of d PPR proteins in complex with their respective ss RNA-targets. The d PPR repeats are assembled into a right-handed superhelical spiral shell that embraces the ss RNA inside. Interactions between different PPR codes and RNA bases are observed at the atomic level, revealing the molecular basis for the modular and specific recognition patterns of the RNA bases U, C, A and G. These structures not only provide insights into the functional study of PPR proteins, but also pinpoint a pathway toward the potential design of synthetic sequence-specific RNA-binding proteins.
As a large family of RNA binding proteins, pentatricopeptide repeat(PPR) proteins mediate multiple aspects of RNA metabolism in eukaryotes. Binding to their target single-stranded RNA(ss RNA) in a modular and base-specific fashion, PPR proteins can serve as designable modules for gene manipulation. However, the structural basis for nucleotide-specific recognition by designer PPR(d PPR) remains to be elucidated. Here we report four crystal structures of d PPR proteins in complex with their respective ss RNA-targets. The d PPR repeats are assembled into a right-handed superhelical spiral shell that embraces the ss RNA inside. Interactions between different PPR codes and RNA bases are observed at the atomic level, revealing the molecular basis for the modular and specific recognition patterns of the RNA bases U, C, A and G. These structures not only provide insights into the functional study of PPR proteins, but also pinpoint a pathway toward the potential design of synthetic sequence-specific RNA-binding proteins.
As a large family of RNA binding proteins, pentatricopeptide repeat(PPR) proteins mediate multiple aspects of RNA metabolism in eukaryotes. Binding to their target single-stranded RNA(ss RNA) in a modular and base-specific fashion, PPR proteins can serve as designable modules for gene manipulation. However, the structural basis for nucleotide-specific recognition by designer PPR(d PPR) remains to be elucidated. Here we report four crystal structures of d PPR proteins in complex with their respective ss RNA-targets. The d PPR repeats are assembled into a right-handed superhelical spiral shell that embraces the ss RNA inside. Interactions between different PPR codes and RNA bases are observed at the atomic level, revealing the molecular basis for the modular and specific recognition patterns of the RNA bases U, C, A and G. These structures not only provide insights into the functional study of PPR proteins, but also pinpoint a pathway toward the potential design of synthetic sequence-specific RNA-binding proteins.
引文