When proteome meets genome: the alpha helix and the beta strand of proteins are eschewed by mRNA splice junctions and may define the minimal indivisible modules of protein architecture.

When proteome meets genome: the alpha helix and the beta strand of proteins are eschewed by mRNA splice junctions and may define the minimal indivisible modules of protein architecture.
复制标题

当蛋白质组遇到基因组时:蛋白质的 α 螺旋和 β 链被 mRNA 剪接点避开,并可能定义蛋白质结构的最小不可分割模块。

DOI:
10.1007/bf02702608
复制
发表时间:
2004
影响因子:
2.9
通讯作者:
Barik,Sailen
Barik,Sailen
中科院分区:
生物学4区
文献类型:
--
作者:
Barik,Sailen

文献摘要

相似文献

基因的内含子-外显子结构的意义是一个谜。由于真核生物蛋白质是由模块化的功能结构域组成的,每个外显子被怀疑编码某种形式的模块;然而,模块的定义仍然模糊。前体mRNA剪接点与来自不同真核生物的蛋白质产物的三维结构的比较显示,与连接蛋白质的更灵活的接头区域(“转角”和“环”)内相比,接头更不可能发生在蛋白质的α-螺旋和B-链内。剪接点均匀分布在不同类型的接头和整个接头序列中,尽管观察到对接头中心区域的轻微偏好。剪接点对α-螺旋和β-链的回避表明存在一种选择压力来阻止它们的破坏,这也许强调了自然界在构建这些复杂的二级结构方面所做的投资。一个推论是螺旋和链是蛋白质最小的整体结构单元,代表蛋白质结构进化中的最小模块。这些结果将在比较基因组学、克隆策略的设计以及基因组序列与蛋白质结构的相互验证中得到应用。
The significance of the intron-exon structure of genes is a mystery. As eukaryotic proteins are made up of modular functional domains, each exon was suspected to encode some form of module; however, the definition of a module remained vague. Comparison of pre-mRNA splice junctions with the three-dimensional architecture of its protein product from different eukaryotes revealed that the junctions were far less likely to occur inside the α-helices and Β-strands of proteins than within the more flexible linker regions (‘turns’ and ‘loops’) connecting them. The splice junctions were equally distributed in the different types of linkers and throughout the linker sequence, although a slight preference for the central region of the linker was observed. The avoidance of the α-helix and the (Β-strand by splice junctions suggests the existence of a selection pressure against their disruption, perhaps underscoring the investment made by nature in building these intricate secondary structures. A corollary is that the helix and the strand are the smallest integral architectural units of a protein and represent the minimal modules in the evolution of protein structure. These results should find use in comparative genomics, designing of cloning strategies, and in the mutual verification of genome sequences with protein structures.