Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA
Abstract
The spliceosome removes introns from precursor messenger RNA (pre-mRNA) to produce mature mRNA. Prior to catalysis, spliceosomes are assembled de novo onto pre-mRNA substrates. During this assembly process, U6 small nuclear RNA (snRNA) undergoes extensive structural remodeling. The early stages of this remodeling process are chaperoned by U6 snRNP proteins Prp24 and the Lsm2–8 heteroheptameric ring. We now report a structure of the U6 snRNP from Saccharomyces cerevisiae. The structure reveals protein–protein contacts that position Lsm2–8 in close proximity to the chaperone “active site” of Prp24. The structure also shows how the Lsm2–8 ring specifically recognizes U6 snRNA that has been post-transcriptionally modified at its 3' end, thereby elucidating the mechanism by which U6 snRNPs selectively recruit 3' end-processed U6 snRNA into spliceosomes. Additionally, the structure reveals unanticipated homology between the C-terminal regions of Lsm8 and the cytoplasmic Lsm1 protein involved in mRNA decay.
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; National Institutes of Health (NIH); National Science Foundation (NSF)
- OSTI Identifier:
- 1436775
- Grant/Contract Number:
- AC02-06CH11357; P41 GM103403; S10 RR029205 085P1000817; R01 GM065166; R35 GM118131; R35 GM118075; BIR-9512577; S10RR13790
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 9; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; RNA; X-ray crystallography
Citation Formats
Montemayor, Eric J., Didychuk, Allison L., Yake, Allyson D., Sidhu, Gurnimrat K., Brow, David A., and Butcher, Samuel E. Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA. United States: N. p., 2018.
Web. doi:10.1038/s41467-018-04145-4.
Montemayor, Eric J., Didychuk, Allison L., Yake, Allyson D., Sidhu, Gurnimrat K., Brow, David A., & Butcher, Samuel E. Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA. United States. https://doi.org/10.1038/s41467-018-04145-4
Montemayor, Eric J., Didychuk, Allison L., Yake, Allyson D., Sidhu, Gurnimrat K., Brow, David A., and Butcher, Samuel E. Tue .
"Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA". United States. https://doi.org/10.1038/s41467-018-04145-4. https://www.osti.gov/servlets/purl/1436775.
@article{osti_1436775,
title = {Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA},
author = {Montemayor, Eric J. and Didychuk, Allison L. and Yake, Allyson D. and Sidhu, Gurnimrat K. and Brow, David A. and Butcher, Samuel E.},
abstractNote = {The spliceosome removes introns from precursor messenger RNA (pre-mRNA) to produce mature mRNA. Prior to catalysis, spliceosomes are assembled de novo onto pre-mRNA substrates. During this assembly process, U6 small nuclear RNA (snRNA) undergoes extensive structural remodeling. The early stages of this remodeling process are chaperoned by U6 snRNP proteins Prp24 and the Lsm2–8 heteroheptameric ring. We now report a structure of the U6 snRNP from Saccharomyces cerevisiae. The structure reveals protein–protein contacts that position Lsm2–8 in close proximity to the chaperone “active site” of Prp24. The structure also shows how the Lsm2–8 ring specifically recognizes U6 snRNA that has been post-transcriptionally modified at its 3' end, thereby elucidating the mechanism by which U6 snRNPs selectively recruit 3' end-processed U6 snRNA into spliceosomes. Additionally, the structure reveals unanticipated homology between the C-terminal regions of Lsm8 and the cytoplasmic Lsm1 protein involved in mRNA decay.},
doi = {10.1038/s41467-018-04145-4},
journal = {Nature Communications},
number = 1,
volume = 9,
place = {United States},
year = {Tue May 01 00:00:00 EDT 2018},
month = {Tue May 01 00:00:00 EDT 2018}
}
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Pat1 RNA-binding proteins: Multitasking shuttling proteins.
text, January 2019
- Vindry, Caroline; Weil, Dominique; Standart, Nancy
- Apollo - University of Cambridge Repository
Structural basis for the evolution of cyclic phosphodiesterase activity in the U6 snRNA exoribonuclease Usb1
journal, December 2019
- Nomura, Yuichiro; Montemayor, Eric J.; Virta, Johanna M.
- Nucleic Acids Research, Vol. 48, Issue 3
Pat1 RNA‐binding proteins: Multitasking shuttling proteins
journal, May 2019
- Vindry, Caroline; Weil, Dominique; Standart, Nancy
- Wiley Interdisciplinary Reviews: RNA, Vol. 10, Issue 6