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首页> 外文期刊>Molecular biology reports >Comparative proteomic and phosphoproteomic analysis of the silkworm (Bombyx mori) posterior silk gland under high temperature treatment
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Comparative proteomic and phosphoproteomic analysis of the silkworm (Bombyx mori) posterior silk gland under high temperature treatment

机译:高温处理后家蚕后蚕腺的蛋白质组学和磷酸化蛋白质组学比较分析

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摘要

The proteins from the posterior silk gland of silkworm hybrids and their parents reared under high temperatures were studied by using comparative proteomic and phosphoproteomic analysis. A total of 82.07, 6.17 and 11.76 % protein spots showed additivity, overdominance and underdominance patterns, respectively. Fifteen differentially expressed protein spots were identified by peptide mass fingerprinting. Among these, four spots, including sHSPs and prohibitin protein that were directly relevant to heat response, were identified. Eleven protein spots were found to play an important role in silk synthesis, and nine protein spots expressed phosphorylation states. According to Gene ontology and KEGG pathway analysis, these nine spots played an important role in stress-induced signal transduction. Expression of most silk synthesis-related proteins was reduced, whereas stress-responsive proteins increased with heat exposure time in three breeds. Furthermore, most proteins showed under- or overdominance in the hybrids compared to the parents. The results suggested that high temperature could alter the expression of proteins related to silk synthesis and heat response in silkworm. Moreover, differentially expressed proteins occurring in the hybrid and its parents may be the main explanation of the observed heterosis.
机译:通过比较蛋白质组学和磷酸化蛋白质组学分析,研究了在高温下饲养的家蚕杂交后代丝腺及其亲本的蛋白质。共有82.07%,6.17%和11.76%的蛋白斑点分别显示出加性,过高和过低模式。通过肽质量指纹图谱鉴定了十五个差异表达的蛋白斑点。其中,鉴定出与热反应直接相关的四个斑点,包括sHSPs和禁止素蛋白。发现11个蛋白质斑点在丝合成中起重要作用,并且9个蛋白质斑点表达磷酸化状态。根据基因本体论和KEGG通路分析,这9个斑点在应激诱导的信号转导中起着重要作用。在三个品种中,大多数丝合成相关蛋白的表达降低,而应激响应蛋白则随着受热时间的增加而增加。此外,与亲本相比,大多数蛋白质在杂种中表现出不足或占优势。结果表明,高温可能会改变蚕中与蚕丝合成和热响应有关的蛋白质的表达。此外,杂种及其亲本中存在的差异表达蛋白可能是观察到的杂种优势的主要原因。

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