Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA

Montemayor, Eric J.; Didychuk, Allison L.; Yake, Allyson D.; Sidhu, Gurnimrat K.; Brow, David A.; Butcher, Samuel E.

doi:10.1038/s41467-018-04145-4

Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA

Journal Article · Tue May 01 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-04145-4· OSTI ID:1436775

Montemayor, Eric J. ^[1]; Didychuk, Allison L. ^[1]; Yake, Allyson D. ^[1]; Sidhu, Gurnimrat K. ^[1]; Brow, David A. ^[1]; ^[1]

Univ. of Wisconsin, Madison, WI (United States)

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.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: NSF; National Inst. of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Scientific User Facilities Division

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1436775

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 9; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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