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首页> 外文期刊>PLoS Genetics >Differential Use of Signal Peptides and Membrane Domains Is a Common Occurrence in the Protein Output of Transcriptional Units
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Differential Use of Signal Peptides and Membrane Domains Is a Common Occurrence in the Protein Output of Transcriptional Units

机译：信号肽和膜结构域的差异使用是转录单位蛋白质输出中的常见现象。

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Membrane organization describes the orientation of a protein with respect to the membrane and can be determined by the presence, or absence, and organization within the protein sequence of two features: endoplasmic reticulum signal peptides and alpha-helical transmembrane domains. These features allow protein sequences to be classified into one of five membrane organization categories: soluble intracellular proteins, soluble secreted proteins, type I membrane proteins, type II membrane proteins, and multi-spanning membrane proteins. Generation of protein isoforms with variable membrane organizations can change a protein's subcellular localization or association with the membrane. Application of MemO, a membrane organization annotation pipeline, to the FANTOM3 Isoform Protein Sequence mouse protein set revealed that within the 8,032 transcriptional units (TUs) with multiple protein isoforms, 573 had variation in their use of signal peptides, 1,527 had variation in their use of transmembrane domains, and 615 generated protein isoforms from distinct membrane organization classes. The mechanisms underlying these transcript variations were analyzed. While TUs were identified encoding all pairwise combinations of membrane organization categories, the most common was conversion of membrane proteins to soluble proteins. Observed within our high-confidence set were 156 TUs predicted to generate both extracellular soluble and membrane proteins, and 217 TUs generating both intracellular soluble and membrane proteins. The differential use of endoplasmic reticulum signal peptides and transmembrane domains is a common occurrence within the variable protein output of TUs. The generation of protein isoforms that are targeted to multiple subcellular locations represents a major functional consequence of transcript variation within the mouse transcriptome.
机译：膜组织描述了蛋白质相对于膜的方向，可以通过蛋白质序列中两个特征（内质网信号肽和α-螺旋跨膜结构域）的存在与否以及组织来确定。这些功能使蛋白质序列可以分类为五种膜组织类别之一：可溶性细胞内蛋白质，可溶性分泌蛋白质，I型膜蛋白，II型膜蛋白和多跨膜蛋白。具有可变的膜组织的蛋白质同工型的产生可以改变蛋白质的亚细胞定位或与膜的缔合。膜组织注释管道MemO在FANTOM3同工型蛋白序列小鼠蛋白质组中的应用表明，在具有多种蛋白同工型的8,032个转录单位（TU）中，有573个信号肽的用途有所变化，有1,527个其信号肽的用途有所变化跨膜结构域的形成，以及615种来自不同膜组织类别的蛋白质同工型。分析了这些转录变异的潜在机制。虽然鉴定出的TUs编码膜组织类别的所有成对组合，但最常见的是将膜蛋白转化为可溶性蛋白。在我们的高可信度集中观察到，预计有156 TU会同时产生细胞外可溶性和膜蛋白，而有217 TU会同时产生细胞内可溶性和膜蛋白。内质网信号肽和跨膜结构域的差异使用是TU的可变蛋白输出中的常见现象。靶向多个亚细胞位置的蛋白质同工型的产生代表小鼠转录组内转录本变异的主要功能结果。

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