气候变化领域集成服务门户(CCPortal): Structural analyses of an RNA stability element interacting with poly(A)

CCPortal

DOI	10.1073/pnas.2026656118
	Structural analyses of an RNA stability element interacting with poly(A)
	Torabi S.-F.; Chen Y.-L.; Zhang K.; Wang J.; DeGregorio S.J.; Vaidya A.T.; Su Z.; Pabit S.A.; Chiu W.; Pollack L.; A. Steitz J.
发表日期	2021
ISSN	00278424
卷号	118 期号:14
英文摘要	Cis-acting RNA elements are crucial for the regulation of polyadenylated RNA stability. The element for nuclear expression (ENE) contains a U-rich internal loop flanked by short helices. An ENE stabilizes RNA by sequestering the poly(A) tail via formation of a triplex structure that inhibits a rapid deadenylation-dependent decay pathway. Structure-based bioinformatic studies identified numerous ENE-like elements in evolutionarily diverse genomes, including a subclass containing two ENE motifs separated by a short double-helical region (double ENEs [dENEs]). Here, the structure of a dENE derived from a rice transposable element (TWIFB1) before and after poly(A) binding (∼24 kDa and ∼33 kDa, respectively) is investigated. We combine biochemical structure probing, small angle X-ray scattering (SAXS), and cryoelectron microscopy (cryo-EM) to investigate the dENE structure and its local and global structural changes upon poly(A) binding. Our data reveal 1) the directionality of poly(A) binding to the dENE, and 2) that the dENEpoly( A) interaction involves a motif that protects the 3'-most seven adenylates of the poly(A). Furthermore, we demonstrate that the dENE does not undergo a dramatic global conformational change upon poly(A) binding. These findings are consistent with the recently solved crystal structure of a dENE+poly(A) complex [S.-F. Torabi et al., Science 371, eabe6523 (2021)]. Identification of additional modes of poly(A)-RNA interaction opens new venues for better understanding of poly(A) tail biology. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Cryo-EM; Poly(A); RNA stability; RNA triple helix; SAXS
语种	英语
scopus关键词	element; polyadenylic acid; RNA helicase; TWIFB1 protein; unclassified drug; Article; biochemistry; conformational transition; controlled study; cryoelectron microscopy; crystal structure; dENE motif; double stranded RNA binding domain; molecular probe; priority journal; protein binding; protein RNA binding; RNA 3' end processing; RNA stability; RNA structure; structure analysis; X ray crystallography
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180002
作者单位	Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06536, United States; HHMI, Yale University, School of Medicine, New Haven, CT 06536, United States; School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853, United States; Department of Bioengineering, Stanford University, Stanford, CA 94305, United States; James H. Clark Center, Stanford University, Stanford, CA 94305, United States; Tata Institute of Fundamental Research Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research, Hyderabad, 10 500046, India; Division of CryoEM and Bioimaging, Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States
推荐引用方式 GB/T 7714	Torabi S.-F.,Chen Y.-L.,Zhang K.,et al. Structural analyses of an RNA stability element interacting with poly(A)[J],2021,118(14).
APA	Torabi S.-F..,Chen Y.-L..,Zhang K..,Wang J..,DeGregorio S.J..,...&A. Steitz J..(2021).Structural analyses of an RNA stability element interacting with poly(A).Proceedings of the National Academy of Sciences of the United States of America,118(14).
MLA	Torabi S.-F.,et al."Structural analyses of an RNA stability element interacting with poly(A)".Proceedings of the National Academy of Sciences of the United States of America 118.14(2021).