Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic Tardigrade improve osmotic tolerance of human cells.
Novel mitochondria-targeted heat-soluble proteins identified in the anhydrobiotic Tardigrade improve osmotic tolerance of human cells.
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DOI：
10.1371/journal.pone.0118272
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发表时间：
2015
期刊：
影响因子：
3.7
通讯作者：
Kunieda T
中科院分区：
文献类型：
--
作者：
Tanaka S;Tanaka J;Miwa Y;Horikawa DD;Katayama T;Arakawa K;Toyoda A;Kubo T;Kunieda T
缓步动物能够忍受几乎完全脱水，通过过渡到代谢不活跃的状态，称为“无水”。胚发育晚期丰度蛋白（LEA）是一种热溶性蛋白，与许多无水生物的脱水耐受有关。然而，缓步动物Ramazzottius varieornatus主要表达缓步动物特有的热溶蛋白：CAHS （Cytoplasmic Abundant Heat Soluble）和SAHS （Secretory Abundant Heat Soluble）蛋白，这些蛋白分泌或定位于除线粒体外的大多数细胞内区室。虽然线粒体的完整性对确保细胞存活至关重要，但线粒体的保护分子仍然难以捉摸。在这里，我们鉴定了两种新的线粒体热溶蛋白，RvLEAM和MAHS（线粒体丰富的热溶蛋白），作为有效的线粒体保护剂。RvLEAM是一种3组LEA蛋白，免疫组化证实其在缓步动物细胞中的线粒体定位。mahs -绿色荧光蛋白融合蛋白定位于人线粒体，在体外可热溶，但与其他已知蛋白没有序列相似性，并且一个区域在缓步动物中保守。此外，我们证明RvLEAM蛋白和MAHS蛋白改善了人类细胞的高渗耐受性。本研究的结果表明，缓步动物线粒体含有至少两种类型的热溶性蛋白质，可能在缺水环境中具有保护作用。
Tardigrades are able to tolerate almost complete dehydration through transition to a metabolically inactive state, called “anhydrobiosis”. Late Embryogenesis Abundant (LEA) proteins are heat-soluble proteins involved in the desiccation tolerance of many anhydrobiotic organisms. Tardigrades, Ramazzottius varieornatus, however, express predominantly tardigrade-unique heat-soluble proteins: CAHS (Cytoplasmic Abundant Heat Soluble) and SAHS (Secretory Abundant Heat Soluble) proteins, which are secreted or localized in most intracellular compartments, except the mitochondria. Although mitochondrial integrity is crucial to ensure cellular survival, protective molecules for mitochondria have remained elusive. Here, we identified two novel mitochondrial heat-soluble proteins, RvLEAM and MAHS (Mitochondrial Abundant Heat Soluble), as potent mitochondrial protectants from Ramazzottius varieornatus. RvLEAM is a group3 LEA protein and immunohistochemistry confirmed its mitochondrial localization in tardigrade cells. MAHS-green fluorescent protein fusion protein localized in human mitochondria and was heat-soluble in vitro, though no sequence similarity with other known proteins was found, and one region was conserved among tardigrades. Furthermore, we demonstrated that RvLEAM protein as well as MAHS protein improved the hyperosmotic tolerance of human cells. The findings of the present study revealed that tardigrade mitochondria contain at least two types of heat-soluble proteins that might have protective roles in water-deficient environments.
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影响因子：
5.8
作者：
Förster F;Beisser D;Grohme MA;Liang C;Mali B;Siegl AM;Engelmann JC;Shkumatov AV;Schokraie E;Müller T;Schnölzer M;Schill RO;Frohme M;Dandekar T
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影响因子：
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作者：
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