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DOI | 10.1126/science.aai7825 |
Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability | |
Leuenberger, Pascal1,2,3; Ganscha, Stefan2,3,4; Kahraman, Abdullah5,6; Cappelletti, Valentina1; Boersema, Paul J.1; von Mering, Christian5,6; Claassen, Manfred4; Picotti, Paola1 | |
2017-02-24 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 355期号:6327 |
文章类型 | Article |
语种 | 英语 |
国家 | Switzerland |
英文摘要 | Temperature-induced cell death is thought to be due to protein denaturation, but the determinants of thermal sensitivity of proteomes remain largely uncharacterized. We developed a structural proteomic strategy to measure protein thermostability on a proteome-wide scale and with domain-level resolution. We applied it to Escherichia coli, Saccharomyces cerevisiae, Thermus thermophilus, and human cells, yielding thermostability data for more than 8000 proteins. Our results (i) indicate that temperature-induced cellular collapse is due to the loss of a subset of proteins with key functions, (ii) shed light on the evolutionary conservation of protein and domain stability, and (iii) suggest that natively disordered proteins in a cell are less prevalent than predicted and (iv) that highly expressed proteins are stable because they are designed to tolerate translational errors that would lead to the accumulation of toxic misfolded species. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000395127600033 |
WOS关键词 | SACCHAROMYCES-CEREVISIAE ; EXPRESSION LEVELS ; STABILITY ; AGGREGATION ; PREDICTION ; BINDING ; TEMPERATURE ; ANNOTATION ; SOLUBILITY ; MECHANISMS |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/195497 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.ETHZ, Dept Biol, Inst Biochem, CH-8093 Zurich, Switzerland; 2.ETHZ, Syst Biol Grad Sch PhD Program, CH-8093 Zurich, Switzerland; 3.Univ Zurich, CH-8093 Zurich, Switzerland; 4.ETHZ, Dept Biol, Inst Mol Syst Biol, CH-8093 Zurich, Switzerland; 5.Univ Zurich, Inst Mol Life Sci, CH-8057 Zurich, Switzerland; 6.Univ Zurich, Swiss Inst Bioinformat, CH-8057 Zurich, Switzerland |
推荐引用方式 GB/T 7714 | Leuenberger, Pascal,Ganscha, Stefan,Kahraman, Abdullah,et al. Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability[J]. SCIENCE,2017,355(6327). |
APA | Leuenberger, Pascal.,Ganscha, Stefan.,Kahraman, Abdullah.,Cappelletti, Valentina.,Boersema, Paul J..,...&Picotti, Paola.(2017).Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability.SCIENCE,355(6327). |
MLA | Leuenberger, Pascal,et al."Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability".SCIENCE 355.6327(2017). |
条目包含的文件 | 条目无相关文件。 |
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