Schümperli, Daniel; Pillai, R S (2004). The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein. Cellular and molecular life sciences, 61(19-20), pp. 2560-2570. Birkhäuser-Verlag; www.birkhauser.ch 10.1007/s00018-004-4190-0
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The polypeptide composition of the U7 small nuclear ribonucleoprotein (snRNP) involved in histone messenger RNA (mRNA) 3' end formation has recently been elucidated. In contrast to spliceosomal snRNPs, which contain a ring-shaped assembly of seven so-called Sm proteins, in the U7 snRNP the Sm proteins D1 and D2 are replaced by U7-specific Sm-like proteins, Lsm10 and Lsm11. This polypeptide composition and the unusual structure of Lsm11, which plays a role in histone RNA processing, represent new themes in the biology of Sm/Lsm proteins. Moreover this structure has important consequences for snRNP assembly that is mediated by two complexes containing the PRMT5 methyltransferase and the SMN (survival of motor neurons) protein, respectively. Finally, the ability to alter this polypeptide composition by a small mutation in U7 snRNA forms the basis for using modified U7 snRNA derivatives to alter specific pre-mRNA splicing events, thereby opening up a new way for antisense gene therapy.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Biology > Institute of Cell Biology |
UniBE Contributor: |
Schümperli, Daniel |
Subjects: |
500 Science > 570 Life sciences; biology |
ISSN: |
1420-682X |
Publisher: |
Birkhäuser-Verlag; www.birkhauser.ch |
Language: |
English |
Submitter: |
Daniel Schümperli |
Date Deposited: |
11 May 2015 17:29 |
Last Modified: |
05 Dec 2022 14:47 |
Publisher DOI: |
10.1007/s00018-004-4190-0 |
PubMed ID: |
15526162 |
BORIS DOI: |
10.7892/boris.68849 |
URI: |
https://boris.unibe.ch/id/eprint/68849 |
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