 |
PDBsum entry 6aso
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
369 a.a.
|
|
|
|
|
|
|
|
|
|
|
95 a.a.
|
|
|
|
|
|
|
|
|
|
|
79 a.a.
|
|
|
|
|
|
|
|
|
|
|
59 a.a.
|
|
|
|
|
|
|
|
|
|
|
79 a.a.
|
|
|
|
|
|
|
|
|
|
|
75 a.a.
|
|
|
|
|
|
|
|
|
|
|
67 a.a.
|
|
|
|
|
|
|
|
|
|
|
83 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Architecture of the u6 snrnp reveals specific recognition of 3'-End processed u6 snrna.
|
|
|
Authors
|
|
E.J.Montemayor,
A.L.Didychuk,
A.D.Yake,
G.K.Sidhu,
D.A.Brow,
S.E.Butcher.
|
|
|
Ref.
|
|
Nat Commun, 2018,
9,
1749.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
