Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii.
Substrates of the chloroplast small heat shock proteins 22E/F point to thermolability as a regulative switch for heat acclimation in Chlamydomonas reinhardtii.
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DOI：
10.1007/s11103-017-0672-y
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发表时间：
2017-12
影响因子：
5.1
通讯作者：
Schroda M
中科院分区：
文献类型：
--
作者：
Rütgers M;Muranaka LS;Mühlhaus T;Sommer F;Thoms S;Schurig J;Willmund F;Schulz-Raffelt M;Schroda M
我们已经确定了39个蛋白质，直接或间接相互作用与热胁迫下的叶绿体HSP 22 E/F，从而揭示了热影响叶绿体的过程具有高的信心。在促进蛋白质解折叠的条件下，小热休克蛋白（sHsps）通过整合形成聚集体来防止解折叠蛋白质的不可逆聚集。含有sHsps的聚集体促进了Hsp 70和ClpB/Hsp 104分子伴侣的进入，这些分子伴侣在ATP依赖性反应中将单个蛋白质从聚集体中解缠结并帮助它们重折叠至天然状态。莱茵衣藻编码8种不同的sHsps（HSP 22 A至H）。这项工作的目标是确定叶绿体靶向的sHsps在衣原体，并获得一个全面的名单，他们在热应激过程中相互作用的基板，以了解哪些叶绿体过程中受到干扰的热应激。我们发现，热休克蛋白22 E和热休克蛋白22 F是主要的叶绿体靶向的sHsps，已经出现了从最近的基因重复事件，导致在团藻目sHsps的持续多样化。HSP 22 E/F在热应激过程中大量积累，形成高分子量复合物。使用差异免疫沉淀，质谱和严格的过滤算法，我们确定了39个蛋白质，具有高置信度直接或间接与热应激下的HSP 22 E/F相互作用。我们建议，这些蛋白质的几个明显的热不稳定性可能是一个理想的性状作为一种机制，使衣原体叶绿体迅速反应热应力的一部分。本文的在线版本（doi：10.1007/s11103-017-0672-y）包含补充材料，可供授权用户使用。
We have identified 39 proteins that interact directly or indirectly with high confidence with chloroplast HSP22E/F under heat stress thus revealing chloroplast processes affected by heat. Under conditions promoting protein unfolding, small heat shock proteins (sHsps) prevent the irreversible aggregation of unfolding proteins by integrating into forming aggregates. Aggregates containing sHsps facilitate the access of Hsp70 and ClpB/Hsp104 chaperones, which in ATP-dependent reactions disentangle individual proteins from the aggregates and assist in their refolding to the native state. Chlamydomonas reinhardtii encodes eight different sHsps (HSP22A to H). The goal of this work was to identify chloroplast-targeted sHsps in Chlamydomonas and to obtain a comprehensive list of the substrates with which they interact during heat stress in order to understand which chloroplast processes are disturbed under heat stress. We show that HSP22E and HSP22F are major chloroplast-targeted sHsps that have emerged from a recent gene duplication event resulting from the ongoing diversification of sHsps in the Volvocales. HSP22E/F strongly accumulate during heat stress and form high molecular mass complexes. Using differential immunoprecipitation, mass spectrometry and a stringent filtering algorithm we identified 39 proteins that with high-confidence interact directly or indirectly with HSP22E/F under heat stress. We propose that the apparent thermolability of several of these proteins might be a desired trait as part of a mechanism enabling Chlamydomonas chloroplasts to rapidly react to thermal stress. The online version of this article (doi:10.1007/s11103-017-0672-y) contains supplementary material, which is available to authorized users.
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影响因子：
5.3
作者：
Castro-Rodríguez V;García-Gutiérrez A;Cañas RA;Pascual MB;Avila C;Cánovas FM
通讯作者：
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影响因子：
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作者：
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影响因子：
3.3
作者：
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通讯作者：
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DOI：
10.1073/pnas.96.22.12524
发表时间：
1999-10-26
影响因子：
11.1
作者：
Koehl, P;Levitt, M
通讯作者：
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影响因子：
6.6
作者：
Hannemann, Liya;Suppanz, Ida;Koch, Hans-Georg
通讯作者：
Koch, Hans-Georg