Bioinformatics Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, 41500, Greece.
Microbial Biotechnology-Molecular Bacteriology-Virology Laboratory, Department of Biochemistry and Biotechnology, University of Thessaly, 41500, Greece.
Nucleic Acids Res. 2019 Nov 4;47(19):9998-10009. doi: 10.1093/nar/gkz730.
We provide the first high-throughput analysis of the properties and functional role of Low Complexity Regions (LCRs) in more than 1500 prokaryotic and phage proteomes. We observe that, contrary to a widespread belief based on older and sparse data, LCRs actually have a significant, persistent and highly conserved presence and role in many and diverse prokaryotes. Their specific amino acid content is linked to proteins with certain molecular functions, such as the binding of RNA, DNA, metal-ions and polysaccharides. In addition, LCRs have been repeatedly identified in very ancient, and usually highly expressed proteins of the translation machinery. At last, based on the amino acid content enriched in certain categories, we have developed a neural network web server to identify LCRs and accurately predict whether they can bind nucleic acids, metal-ions or are involved in chaperone functions. An evaluation of the tool showed that it is highly accurate for eukaryotic proteins as well.
我们提供了对超过 1500 种原核生物和噬菌体蛋白质组中低复杂度区域(LCRs)的特性和功能作用的首次高通量分析。我们观察到,与基于旧的和稀疏数据的普遍观点相反,LCRs 实际上在许多不同的原核生物中具有显著、持久和高度保守的存在和作用。它们的特定氨基酸含量与具有某些分子功能的蛋白质相关联,例如 RNA、DNA、金属离子和多糖的结合。此外,LCRs 已在非常古老且通常高度表达的翻译机制蛋白中反复被识别出来。最后,基于在某些类别中富集的氨基酸含量,我们开发了一个神经网络网络服务器来识别 LCRs,并准确预测它们是否可以结合核酸、金属离子或参与伴侣功能。该工具的评估表明,它对真核蛋白也具有高度准确性。