Determining translocation orientations of nucleic acid helicases

被引:0
|
作者
Perera, Himasha M. [1 ]
Trakselis, Michael A. [1 ]
机构
[1] Baylor Univ, Dept Chem & Biochem, Waco, TX 76798 USA
基金
美国国家科学基金会;
关键词
DNA replication; MCM helicase; Translocation; Unwinding; Polarity; Orientation; INDUCED FLUORESCENCE ENHANCEMENT; STRANDED-DNA TRANSLOCATION; EUKARYOTIC CMG HELICASE; COLI REP HELICASE; ESCHERICHIA-COLI; REPLICATION FORK; SINGLE-MOLECULE; STRUCTURAL BASIS; RIG-I; CRYSTAL-STRUCTURE;
D O I
10.1016/j.ymeth.2021.11.001
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Helicase enzymes translocate along an RNA or DNA template with a defined polarity to unwind, separate, or remodel duplex strands for a variety of genome maintenance processes. Helicase mutations are commonly associated with a variety of diseases including aging, cancer, and neurodegeneration. Biochemical characterization of these enzymes has provided a wealth of information on the kinetics of unwinding and substrate preferences, and several high-resolution structures of helicases alone and bound to oligonucleotides have been solved. Together, they provide mechanistic insights into the structural translocation and unwinding orientations of helicases. However, these insights rely on structural inferences derived from static snapshots. Instead, continued efforts should be made to combine structure and kinetics to better define active translocation orientations of helicases. This review explores many of the biochemical and biophysical methods utilized to map helicase binding orientation to DNA or RNA substrates and includes several time-dependent methods to unequivocally map the active translocation orientation of these enzymes to better define the active leading and trailing faces.
引用
收藏
页码:160 / 171
页数:12
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