Elucidating Protein Translocon Dynamics with Single-Molecule Precision

被引:0
|
作者
Davis, Madeline M. [1 ]
Lamichhane, Rajan [1 ]
Bruce, Barry D. [1 ,2 ,3 ,4 ]
机构
[1] Univ Tennessee, Dept Biochem & Cellular & Mol Biol, Knoxville, TN 37996 USA
[2] Univ Tennessee, Dept Microbiol, Knoxville, TN 37996 USA
[3] Univ Tennessee, Grad Program Genome Sci & Technol, Knoxville, TN 37996 USA
[4] Univ Tennessee, Chem & Biomol Engn, Knoxville, TN 37996 USA
基金
美国国家科学基金会;
关键词
CRYO-EM STRUCTURE; FORCE SPECTROSCOPY; TRANSIT PEPTIDE; ESCHERICHIA-COLI; IN-VIVO; OPTICAL TWEEZERS; OUTER-MEMBRANE; CHANNEL; IMPORT; COMPLEX;
D O I
10.1016/j.tcb.2021.03.009
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Translocons are protein assemblies that facilitate the targeting and transport of proteins into and across biological membranes. Our understanding of these systems has been advanced using genetics, biochemistry, and structural biology. Despite these classic advances, until recently we have still largely lacked a detailed understanding of how translocons recognize and facilitate protein trans location. With the advent and improvements of cryogenic electron microscopy (cryo-EM) single-particle analysis and single-molecule fluorescence microscopy, the details of how translocons function are finally emerging. Here, we introduce these methods and evaluate their importance in understanding translocon structure, function, and dynamics.
引用
收藏
页码:569 / 583
页数:15
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