主题:【分享】细胞是如何出口和嵌入蛋白于细胞膜

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细胞是如何出口和嵌入蛋白于细胞膜
Grenoble, 12 December 2010
How cells export and embed proteins in the membrane
EMBL scientists first to visualise crucial step

http://www.embl.de/aboutus/communication_outreach/media_relations/2010/101212_Grenoble/index.html

Like an overprotective parent on the first day of school, a targeting factor sometimes needs a little push to let go of its cargo. Scientists at the European Molecular Biology Laboratory (EMBL) in Grenoble, France, have visualised one such hand-over. They were the first to determine the structure of a ribosome-protein complex involved in carrying nascent proteins out of the cell. Their work, published online today in Nature Structural and Molecular Biology, could increase understanding of illnesses such as cystic fibrosis and some forms of Parkinson’s disease, in which improper protein targeting leads proteins to harmfully accumulate inside cells.

In most organisms, proteins destined to cross or be embedded in a membrane contain a polypeptide sequence that is recognized during translation by a targeting factor known as the signal recognition particle (SRP). SRP binds to the ribosome synthesizing the polypeptide, and subsequently also binds an SRP receptor, located next to the machinery that transfers proteins across the membrane and out of the cell. EMBL scientists have now generated the first-ever structural image of this important step in the process.

“The SRP receptor acts as a switch between the cargo binding and the release,” says Christiane Schaffitzel, who led the research at EMBL, “Now we have seen for the first time how the release can happen at a molecular level.”

Schaffitzel’s group is taking structural snapshots of entire pathways by which proteins are synthesized and targeted to their final positions. To capture this hand-over step, the scientists had to overcome the fact that the link between SRP and its receptor is usually transient, chemically unstable. They engineered the SRP receptor so that it would bind more stably to SRP, then introduced ribosomes and observed the resulting complexes using cryo-electron microscopy (cryo-EM).

Cryo-EM can be performed in roughly physiological conditions, providing a picture that closely resembles what happens in living cells. This picture can then be combined with higher-resolution crystallography data and biochemical studies – an exciting hybrid approach the EMBL scientists will further exploit to follow protein targeting all the way from start to finish.A particular asset for success in this project was the close collaboration with Guy Schoehn at the Institut de Biologie Structurale (IBS). IBS and EMBL are part of the Partnership for Structural Biology (PS15, in Grenoble, France.

Source Article
Estrozi, L.F., Boehringer, D., Shan, S., Ban, N., Schaffitzel, C.. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nature Structural and Molecular Biology, Advance Online Publication 12 December 2010. DOI: 10.1038/nsmb.1952.
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细胞是如何出口和嵌入蛋白于细胞膜

Grenoble, 12 December 2010
How cells export and embed proteins in the membrane
EMBL scientists first to visualise crucial step

http://www.embl.de/aboutus/communication_outreach/media_relations/2010/101212_Grenoble/index.html

Like an overprotective parent on the first day of school, a targeting factor sometimes needs a little push to let go of its cargo. Scientists at the European Molecular Biology Laboratory (EMBL) in Grenoble, France, have visualised one such hand-over. They were the first to determine the structure of a ribosome-protein complex involved in carrying nascent proteins out of the cell. Their work, published online today in Nature Structural and Molecular Biology, could increase understanding of illnesses such as cystic fibrosis and some forms of Parkinson’s disease, in which improper protein targeting leads proteins to harmfully accumulate inside cells.
就像过度呵护孩子父母在开学的第一天那样,有时需要针对目标因子轻轻一推使得其离开原有位置。在法国格勒诺布尔的欧洲分子生物学实验室(EMBL),科学家们可直视这样的一个交接。他们是最早确定参与核糖体蛋白复合体结构新生的细胞蛋白质。他们的工作,今天在《Nature Structural》网络版上发表了一个分子的生物学,可以提高对诸如囊肿性纤维化和某些帕金森氏症的认识,其中这种蛋白质的定位不当导致有害蛋白质在细胞内积累。

In most organisms, proteins destined to cross or be embedded in a membrane contain a polypeptide sequence that is recognized during translation by a targeting factor known as the signal recognition particle (SRP). SRP binds to the ribosome synthesizing the polypeptide, and subsequently also binds an SRP receptor, located next to the machinery that transfers proteins across the membrane and out of the cell. EMBL scientists have now generated the first-ever structural image of this important step in the process.
在大多数生物,蛋白质注定要贯穿或嵌入细胞膜,此膜包含一个多肽序列,在翻译过程中通过信号识别颗粒(SRP)的一个靶因子来识别。 SRP结合到合成的肽的核糖体中,随后和SRP受体结合,定位之处在将蛋白在膜之间转移或者转运出细胞的地方。 EMBL的科学家现在已经开发出了这一进程重要一步的首个结构图像

“The SRP receptor acts as a switch between the cargo binding and the release,” says Christiane Schaffitzel, who led the research at EMBL, “Now we have seen for the first time how the release can happen at a molecular level.”
“SRP受体作为之间的物质结合和和释放过程中的开关”, EMBL领衔这项研究的Christiane Schaffitzel说到,“现在我们在分子水平上看到第一次释放是如何发生的”。

Schaffitzel’s group is taking structural snapshots of entire pathways by which proteins are synthesized and targeted to their final positions. To capture this hand-over step, the scientists had to overcome the fact that the link between SRP and its receptor is usually transient, chemically unstable. They engineered the SRP receptor so that it would bind more stably to SRP, then introduced ribosomes and observed the resulting complexes using cryo-electron microscopy (cryo-EM).
Schaffitzel的研究小组正在对整个通路结构进行快照,通过到达最后位置蛋白的合成和靶定。为了捕捉这交接步骤,科学家们必须克服一个事实,即SRP和其受体之间的联系通常是短暂的,化学性质不稳定。他们设计了SRP受体,这样会更稳定的结合SRP,然后导入了核糖体,并使用低温电子显微镜(冷冻电镜)观察。

Cryo-EM can be performed in roughly physiological conditions, providing a picture that closely resembles what happens in living cells. This picture can then be combined with higher-resolution crystallography data and biochemical studies – an exciting hybrid approach the EMBL scientists will further exploit to follow protein targeting all the way from start to finish.A particular asset for success in this project was the close collaboration with Guy Schoehn at the Institut de Biologie Structurale (IBS). IBS and EMBL are part of the Partnership for Structural Biology (PS in Grenoble, France.
冷冻电镜可以在大致的生理条件进行,提供的图片非常类似于活细胞在体内的过程。这张照片然后可以结合高解析度晶体学数据和生化研究 - 一个令人兴奋的混合方法使得EMBL的科学家进一步利用蛋白质始终能定位跟踪。这个项目成功是和生物结构研究所(IBS)Schoehn的密切合作。 IBS和EMBL是结构生物学的伙伴关系(在法国的格勒诺布尔)。

Source Article
Estrozi, L.F., Boehringer, D., Shan, S., Ban, N., Schaffitzel, C.. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nature Structural and Molecular Biology, Advance Online Publication 12 December 2010. DOI: 10.1038/nsmb.1952.

文章的来源
Estrozi, L.F., Boehringer, D., Shan, S., Ban, N., Schaffitzel, C.. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nature Structural and Molecular Biology, Advance Online Publication 12 December 2010. DOI: 10.1038/nsmb.1952.
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题目 细胞在细胞膜中如何通过和嵌入

编译 zfyyzz00

字数 671个



就像过度呵护孩子父母在开学的第一天那样,有时需要针对目标因子轻轻一推使得其离开原有位置。在法国格勒诺布尔的欧洲分子生物学实验室(EMBL),科学家们可直视这样的一个交接。他们是最早确定参与核糖体蛋白复合体结构新生的细胞蛋白质。他们的工作,今天在《Nature Structural》网络版上发表了一个分子的生物学,可以提高对诸如囊肿性纤维化和某些帕金森氏症的认识,其中这种蛋白质的定位不当导致有害蛋白质在细胞内积累。

在大多数生物,蛋白质注定要贯穿或嵌入细胞膜,此膜包含一个多肽序列,在翻译过程中通过信号识别颗粒(SRP)的一个靶因子来识别。 SRP结合到合成的肽的核糖体中,随后和SRP受体结合,定位之处存在将蛋白在膜内转移或者转运出细胞的地方。 EMBL的科学家现在已经开发出了这一进程重要一步的首个结构图像

“SRP受体作为物质之间结合和释放的开关”, EMBL领衔这项研究的Christiane Schaffitzel说到,“现在我们首次在分子水平上看到释放是如何发生的”。

Schaffitzel的研究小组通过到达最后位置蛋白的合成和靶定正在对整个通路结构进行快照。为了捕捉这交接步骤,科学家们必须攻克一个难题,即SRP和其受体之间的联系通常是短暂的,化学性质不稳定。他们设计了SRP受体,这样会更稳定的结合SRP,然后导入了核糖体,并使用低温电子显微镜(冷冻电镜)观察。

冷冻电镜可以在大致生理条件进行,提供的图片非常类似于活细胞在体内的过程。这张照片然后可以结合高解析度晶体学数据和生化研究 - 一个令人振奋的结合方法使得EMBL的科学家进一步利用蛋白质始终能定位跟踪。这个项目成功是和生物结构研究所(IBS)Schoehn密切合作的结果。 IBS和EMBL是结构生物学的伙伴关系(在法国的格勒诺布尔)。

文章的来源
Estrozi, L.F., Boehringer, D., Shan, S., Ban, N., Schaffitzel, C.. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nature Structural and Molecular Biology, Advance Online Publication 12 December 2010. DOI: 10.1038/nsmb.1952.

http://www.embl.de/aboutus/communication_outreach/media_relations/2010/101212_Grenoble/index.html
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还好有中文对照着,看起来好一点。要不太累了。