Pillai, R S; Will, C L; Lührmann, R; Schümperli, Daniel; Müller, B (2001). Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein. EMBO journal, 20(19), pp. 5470-5479. Nature Publishing Group 10.1093/emboj/20.19.5470
Full text not available from this repository.U7 snRNPs were isolated from HeLa cells by biochemical fractionation, followed by affinity purification with a biotinylated oligonucleotide complementary to U7 snRNA. Purified U7 snRNPs lack the Sm proteins D1 and D2, but contain additional polypeptides of 14, 50 and 70 kDa. Microsequencing identified the 14 kDa polypeptide as a new Sm-like protein related to Sm D1 and D3. Like U7 snRNA, this protein, named Lsm10, is enriched in Cajal bodies of the cell nucleus. Its incorporation into U7 snRNPs is largely dictated by the special Sm binding site of U7 snRNA. This novel type of Sm complex, composed of both conventional Sm proteins and the Sm-like Lsm10, is most likely to be important for U7 snRNP function and subcellular localization.
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: |
0261-4189 |
Publisher: |
Nature Publishing Group |
Language: |
English |
Submitter: |
Daniel Schümperli |
Date Deposited: |
08 May 2015 11:36 |
Last Modified: |
05 Dec 2022 14:47 |
Publisher DOI: |
10.1093/emboj/20.19.5470 |
PubMed ID: |
11574479 |
URI: |
https://boris.unibe.ch/id/eprint/68856 |
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