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Relationship between Type I and Type II Template Processes: Amyloids and Genome Stability
Molecular Biology ( IF 1.2 ) Pub Date : 2020-10-19 , DOI: 10.1134/s0026893320050027
Yu. V. Andreychuk , S. P. Zadorsky , A. S. Zhuk , E. I. Stepchenkova , S. G. Inge-Vechtomov

Abstract

Classical views of hereditary mechanisms consider linear nucleic acids, DNA and RNA, as template molecules wherein genetic information is encoded by the sequence of nitrogenous bases. The template principle embodied in the central dogma of molecular biology describes the allowed paths of genetic information transfer from nucleic acids to proteins. The discovery of prions revealed an additional hereditary mechanism whereby the spatial structure is transmitted from one protein molecule to another independently of the sequence of nitrogenous bases in their structural genes. The simultaneous existence of linear (type I) and conformational (type II) templates in one cell inevitably implies their interaction. The review analyzes the current data confirming the idea that protein amyloid transformation may influence the genome stability and considers potential mechanisms of interactions between type I and type II template processes. Special attention is paid to the joint contribution of the two process to tumor “evolution” and the mechanisms of genome destabilization due to amyloid transformation of proteins in Alzheimer’s and Parkinson’s diseases and Down syndrome.



中文翻译:

I型和II型模板过程之间的关系:淀粉样蛋白和基因组稳定性

摘要

遗传机制的经典观点认为线性核酸,DNA和RNA是模板分子,其中遗传信息由含氮碱基序列编码。分子生物学中心教义中体现的模板原理描述了遗传信息从核酸转移到蛋白质的允许途径。ions病毒的发现揭示了另一种遗传机制,其中空间结构从一个蛋白质分子传递到另一个蛋白质分子,而与它们结构基因中的氮碱基序列无关。一个单元中线性(I型)和构象(II型)模板的同时存在不可避免地暗示着它们的相互作用。该评论分析了目前的数据,确认了蛋白质淀粉样蛋白转化可能影响基因组稳定性的想法,并考虑了I型和II型模板过程之间相互作用的潜在机制。特别要注意这两个过程对肿瘤“进化”的共同贡献,以及由于阿尔茨海默氏病和帕金森氏病和唐氏综合症中蛋白质的淀粉样变性导致的基因组失稳机制。

更新日期:2020-10-19
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