期刊
ANNUAL REVIEW OF BIOPHYSICS, VOL 41
卷 41, 期 -, 页码 247-267出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-050511-102243
关键词
ATPase; helicase; molecular motor; kinetics; thermodynamics; mechanism
类别
资金
- NIGMS NIH HHS [R01 GM071688, GM097348, R01 GM097348] Funding Source: Medline
RNA helicase enzymes catalyze the in vivo folding and conformational rearrangement of RNA. DEAD-box proteins (DBPs) make up the largest family of RNA helicases and are found across all phyla. DBPs are molecular motor proteins that utilize chemical energy in cycles of ATP binding, hydrolysis, and product release to perform mechanical work resulting in reorganization of cellular RNAs. DBPs contain a highly conserved motor domain helicase core. Auxiliary domains, enzymatic adaptations, and regulatory partner proteins contribute to the diversity of DBP function throughout RNA metabolism. In this review we focus on the current understanding of the DBP ATP utilization mechanism in rearranging and unwinding RNA structures. We discuss DBP structural properties, kinetic pathways, and thermodynamic features of nucleotide-dependent interactions with RNA. We highlight recent advances in the DBP field derived from biochemical and molecular biophysical investigations aimed at developing a quantitative mechanistic understanding of DBP molecular motor function.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据