Rng3, a member of the UCS family of myosin co-chaperones, associates with myosin heavy chains cotranslationally

Rng3, a member of the UCS family of myosin co-chaperones, associates with myosin heavy chains cotranslationally
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DOI:
10.1038/embor.2008.228
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发表时间:
2009-02-01
期刊:
影响因子:
7.7
通讯作者:
Mata, Juan
Mata, Juan
中科院分区:
生物学2区
文献类型:
--
作者:
Amorim, Maria J.;Mata, Juan

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在许多真核生物中,功能性肌球蛋白重链的产生需要含UCS结构域(UNC - 45/CRO1/She4)的蛋白质发挥作用,这些蛋白质与肌球蛋白头部结构域结合并促进其折叠。UCS蛋白对于与肌球蛋白相关的功能(如肌肉形成、RNA定位和胞质分裂)至关重要。在此,我们发现粟酒裂殖酵母的UCS蛋白Rng3与多聚核糖体相关联,这表明UCS蛋白可能在共翻译过程中协助肌球蛋白折叠。为了系统地确定Rng3的共翻译靶点,我们纯化了与Rng3相关的RNA,并使用DNA微阵列来鉴定转录本。Rng3仅与7种转录本(约占粟酒裂殖酵母基因的0.1%)共纯化,包括编码肌球蛋白重链的所有5种信使RNA。这些结果表明,粟酒裂殖酵母中的每一种肌球蛋白重链都是Rng3的共翻译靶点。此外,我们的数据表明,基于微阵列的方法能够在全基因组范围内鉴定共翻译伴侣蛋白的靶点,从而为剖析与翻译相关的伴侣蛋白网络铺平了道路。
The production of functional myosin heavy chains in many eukaryotic organisms requires the function of proteins containing UCS domains (UNC-45/CRO1/She4), which bind to the myosin head domain and stimulate its folding. UCS proteins are essential for myosin-related functions such as muscle formation, RNA localization and cytokinesis. Here, we show that the Schizosaccharomyces pombe UCS protein Rng3 associates with polysomes, suggesting that UCS proteins might assist myosin folding cotranslationally. To identify Rng3 cotranslational targets systematically, we purified Rng3-associated RNAs and used DNA microarrays to identify the transcripts. Rng3 copurified with only seven transcripts (around 0.1% of S. pombe genes), including all five messenger RNAs encoding myosin heavy chains. These results suggest that every myosin heavy chain in S. pombe is a cotranslational target of Rng3. Furthermore, our data suggest that microarray-based approaches allow the genome-wide identification of cotranslational chaperone targets, and thus pave the way for the dissection of translation-linked chaperone networks.