Journal
TRENDS IN CELL BIOLOGY
Volume 31, Issue 7, Pages 569-583Publisher
CELL PRESS
DOI: 10.1016/j.tcb.2021.03.009
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Funding
- Gibson Family Foundation
- Dr Donald L. Akers Faculty Enrichment Fellowship
- National Science Foundation [EPS-1004083, MRI1828300]
- UTK/ORNL Science Alliance
- Science Alliance at University of Tennessee, Knoxville
- ORE SARIF funds
- College of Arts and Sciences, University of Tennessee, Knoxville
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Translocons are protein assemblies that aid in protein targeting and transport across biological membranes. Recent advancements in cryogenic electron microscopy and single-molecule fluorescence microscopy have allowed for a more detailed understanding of translocon function. These methods are crucial in studying the structure, function, and dynamics of translocons.
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.
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