Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing.

Pillai, Ramesh S; Grimmler, Matthias; Meister, Gunter; Will, Cindy L; Lührmann, Reinhard; Fischer, Utz; Schümperli, Daniel (2003). Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing. Genes & development, 17(18), pp. 2321-2333. Cold Spring Harbor Laboratory Press 10.1101/gad.274403

[img] Text
Schümperli.pdf - Published Version
Restricted to registered users only
Available under License Publisher holds Copyright.

Download (538kB) | Request a copy

A set of seven Sm proteins assemble on the Sm-binding site of spliceosomal U snRNAs to form the ring-shaped Sm core. The U7 snRNP involved in histone RNA 3' processing contains a structurally similar but biochemically unique Sm core in which two of these proteins, Sm D1 and D2, are replaced by Lsm10 and by another as yet unknown component. Here we characterize this factor, termed Lsm11, as a novel Sm-like protein with apparently two distinct functions. In vitro studies suggest that its long N-terminal part mediates an important step in histone mRNA 3'-end cleavage, most likely by recruiting a zinc finger protein previously identified as a processing factor. In contrast, the C-terminal part, which comprises two Sm motifs interrupted by an unusually long spacer, is sufficient to assemble with U7, but not U1, snRNA. Assembly of this U7-specific Sm core depends on the noncanonical Sm-binding site of U7 snRNA. Moreover, it is facilitated by a specialized SMN complex that contains Lsm10 and Lsm11 but lacks Sm D1/D2. Thus, the U7-specific Lsm11 protein not only specifies the assembly of the U7 Sm core but also fulfills an important role in U7 snRNP-mediated histone mRNA processing.

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:

0890-9369

Publisher:

Cold Spring Harbor Laboratory Press

Language:

English

Submitter:

Daniel Schümperli

Date Deposited:

12 May 2015 08:24

Last Modified:

12 May 2015 09:13

Publisher DOI:

10.1101/gad.274403

PubMed ID:

12975319

BORIS DOI:

10.7892/boris.68852

URI:

https://boris.unibe.ch/id/eprint/68852

Actions (login required)

Edit item Edit item
Provide Feedback