Proteome plasticity in response to persistent environmental change.

Proteome plasticity in response to persistent environmental change.
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DOI:
10.1016/j.molcel.2021.06.028
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发表时间:
2021-08-19
期刊:
影响因子:
16
通讯作者:
Zhou C
Zhou C
中科院分区:
生物学1区
文献类型:
--
作者:
Domnauer M;Zheng F;Li L;Zhang Y;Chang CE;Unruh JR;Conkright-Fincham J;McCroskey S;Florens L;Zhang Y;Seidel C;Fong B;Schilling B;Sharma R;Ramanathan A;Si K;Zhou C

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Temperature is a variable component of the environment and all organisms must deal with or adapt to temperature change. Acute temperature change activates cellular stress responses resulting in the refolding or removal of damaged proteins. However, how organisms adapt to long-term temperature change remains largely unexplored. Here, we report that budding yeast responds to long-term high temperature challenge by switching from chaperone induction to the reduction of temperature sensitive proteins and re-localizing a portion of its proteome. Surprisingly, we also find that many proteins adopt an alternative conformation. Using Fet3p as an example, we find that the temperature-dependent conformational difference is accompanied by distinct thermostability, subcellular localization, and importantly, cellular functions. We postulate that in addition to the known mechanisms of adaptation, conformational plasticity allows some polypeptides to acquire new biophysical properties and functions when environmental change endures. Domnauer et al. report that budding yeast responds to long-term temperature change by switching from chaperone induction to the reduction of thermolabile proteins and redistribution of some proteins. Long-term temperature shift also induces alternative protein conformations, which is accompanied by distinct thermostability, subcellular localization, and cellular functions for some proteins.
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