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DOI	10.1126/science.aai7825
	Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability
	Leuenberger P.; Ganscha S.; Kahraman A.; Cappelletti V.; Boersema P.J.; Von Mering C.; Claassen M.; Picotti P.
发表日期	2017
ISSN	0036-8075
卷号	355 期号:6327
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. Copyright 2016 by the American Association for the Advancement of Science; all rights reserved.
英文关键词	alpha synuclein; bovine serum albumin; intrinsically disordered protein; peptide fragment; proteinase; proteome; triosephosphate isomerase; trypsin; ubiquitin; protein; bacterium; cells and cell components; coliform bacterium; protein; proteomics; temperature effect; tolerance; yeast; Article; circular dichroism; comparative study; controlled study; Escherichia coli; fatty acid synthesis; human; human cell; mass spectrometry; melting point; nonhuman; priority journal; protein analysis; protein denaturation; protein depletion; protein domain; protein expression; protein metabolism; protein protein interaction; protein secondary structure; protein stability; protein structure; protein synthesis; protein unfolding; proteomics; Saccharomyces cerevisiae; temperature acclimatization; temperature sensitivity; thermophile; thermostability; Thermus thermophilus; transition temperature; chemistry; genetics; metabolism; procedures; protein degradation; temperature; Escherichia coli; Saccharomyces cerevisiae; Thermus thermophilus; Escherichia coli; Humans; Mass Spectrometry; Protein Denaturation; Protein Interaction Maps; Protein Stability; Protein Unfolding; Proteins; Proteolysis; Proteome; Proteomics; Saccharomyces cerevisiae; Temperature; Thermus thermophilus
语种	英语
来源期刊	Science
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/244507
作者单位	Institute of Biochemistry, Department of Biology, ETH Zurich (ETHZ), Zurich, CH-8093, Switzerland; Systems Biology Graduate School PhD Program, ETHZ, University of Zurich, Zurich, CH-8093, Switzerland; Institute of Molecular Systems Biology, Department of Biology, ETHZ, Zurich, CH-8093, Switzerland; Institute of Molecular Life Sciences, Swiss Institute of Bioinformatics, University of Zurich, Zurich, CH-8057, Switzerland
推荐引用方式 GB/T 7714	Leuenberger P.,Ganscha S.,Kahraman A.,et al. Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability[J],2017,355(6327).
APA	Leuenberger P..,Ganscha S..,Kahraman A..,Cappelletti V..,Boersema P.J..,...&Picotti P..(2017).Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability.Science,355(6327).
MLA	Leuenberger P.,et al."Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability".Science 355.6327(2017).