High-resolution cryo-EM on eukaryotic chaperonin TRiC/CCT
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- 英文论文题名：High-resolution cryo-EM on eukaryotic chaperonin TRiC/CCT
- 论文作者：Yunxiang Zang ; Mingliang Jin ; Yao Cong
- 英文论文作者：Yunxiang Zang ; Mingliang Jin ; Yao Cong ; Institute of Biochemistry and Cell Biology ; National Center for Protein Sciences.Shanghai
- 年：2016
- 作者机构：Institute of Biochemistry and Cell Biology,National Center for Protein Sciences.Shanghai;
- 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：Q75
- 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：297k
- 原文格式：D
- 会议级别：全国
摘要
The eukaryotic chaperonin TRiC/CCT involves in the folding of approximately 10%of cytosolic proteins.This ATP-driven macromolecular machine consists of eight distinct but similar subunits.Dysfunction of TRiC is closely associated with cancer or neurodegenerative diseases.Here we present two high-resolution cryo-EM structures of yeast S.cerevisiae TRiC in the apo and nucleotide-bound states.Through internal subunit labeling,we unambiguously identified the subunit locations in the apo state map of TRiC.The apo-TRiC map also reveals an unforeseen conformation of TRiC in this nucleotidefree state.Strikingly,ATP-binding can already induce a dramatic conformational change in some subunits,forming the first-stage towards TRiC ring closure.Moreover,in the nucleotide-binding pocket we can find nucleotide density only in some of the subunits all located in one side of the complex.Combining this observation with the conformational variations,our data indicate that the TRiC complex can be divided into two portions,i.e.subunits in one side of the complex may play a pivotal role in initiating TRiC ring closure;while those in the other side of the complex could be the key players in substrate recognition and folding.In summery,our results reveal the first-stage TRiC ring closure triggered by ATP-binding,and facilitate our understanding on the structural mechanisms of TRiC's highly efficient allosteric cooperativity and functional division of responsibility.
The eukaryotic chaperonin TRiC/CCT involves in the folding of approximately 10%of cytosolic proteins.This ATP-driven macromolecular machine consists of eight distinct but similar subunits.Dysfunction of TRiC is closely associated with cancer or neurodegenerative diseases.Here we present two high-resolution cryo-EM structures of yeast S.cerevisiae TRiC in the apo and nucleotide-bound states.Through internal subunit labeling,we unambiguously identified the subunit locations in the apo state map of TRiC.The apo-TRiC map also reveals an unforeseen conformation of TRiC in this nucleotidefree state.Strikingly,ATP-binding can already induce a dramatic conformational change in some subunits,forming the first-stage towards TRiC ring closure.Moreover,in the nucleotide-binding pocket we can find nucleotide density only in some of the subunits all located in one side of the complex.Combining this observation with the conformational variations,our data indicate that the TRiC complex can be divided into two portions,i.e.subunits in one side of the complex may play a pivotal role in initiating TRiC ring closure;while those in the other side of the complex could be the key players in substrate recognition and folding.In summery,our results reveal the first-stage TRiC ring closure triggered by ATP-binding,and facilitate our understanding on the structural mechanisms of TRiC's highly efficient allosteric cooperativity and functional division of responsibility.
The eukaryotic chaperonin TRiC/CCT involves in the folding of approximately 10%of cytosolic proteins.This ATP-driven macromolecular machine consists of eight distinct but similar subunits.Dysfunction of TRiC is closely associated with cancer or neurodegenerative diseases.Here we present two high-resolution cryo-EM structures of yeast S.cerevisiae TRiC in the apo and nucleotide-bound states.Through internal subunit labeling,we unambiguously identified the subunit locations in the apo state map of TRiC.The apo-TRiC map also reveals an unforeseen conformation of TRiC in this nucleotidefree state.Strikingly,ATP-binding can already induce a dramatic conformational change in some subunits,forming the first-stage towards TRiC ring closure.Moreover,in the nucleotide-binding pocket we can find nucleotide density only in some of the subunits all located in one side of the complex.Combining this observation with the conformational variations,our data indicate that the TRiC complex can be divided into two portions,i.e.subunits in one side of the complex may play a pivotal role in initiating TRiC ring closure;while those in the other side of the complex could be the key players in substrate recognition and folding.In summery,our results reveal the first-stage TRiC ring closure triggered by ATP-binding,and facilitate our understanding on the structural mechanisms of TRiC's highly efficient allosteric cooperativity and functional division of responsibility.
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