TY - JOUR

T1 - Relationship between Type I and Type II Template Processes

T2 - Amyloids and Genome Stability

AU - Andreychuk, Yu V.

AU - Zadorsky, S. P.

AU - Zhuk, A. S.

AU - Stepchenkova, E. I.

AU - Inge-Vechtomov, S. G.

N1 - Publisher Copyright: © 2020, Pleiades Publishing, Inc.

PY - 2020/9/1

Y1 - 2020/9/1

N2 - 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.

AB - 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.

KW - amyloid

KW - amyloid neurodegenerative diseases

KW - aneuploidy

KW - genome stability

KW - mutation

KW - prion

UR - http://www.scopus.com/inward/record.url?scp=85092754996&partnerID=8YFLogxK

U2 - 10.1134/S0026893320050027

DO - 10.1134/S0026893320050027

M3 - Review article

C2 - 33009788

AN - SCOPUS:85092677774

VL - 54

SP - 661

EP - 683

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 5

ER -