Ruepp, Marc-David (11 June 2013). FUS protein interacts with U7 snRNP and plays a role in replication-dependant histone genes expression (Unpublished). In: 18th International Annual Meeting of the RNA Society. 11.-15.06.2013.
The U7 small nuclear ribonucleoprotein (U7 snRNP) is an essential factor mediating the unique 3’end processing of non-polyadenylated, replication-dependent histone mRNAs in metazoans. These histone genes expression and processing of their transcripts are cell cycle-regulated mechanisms that recruit a number of specific proteins as well as common factors required for expression and maturation of polyadenylated mRNAs. However, despite all the knowledge we have so far, there are still gaps in understanding of core histone RNA 3’ end processing, its coupling to transcription and regulation during cell cycle. To further elucidate this phenomena we used affinity chromatography based on tagged version of U7 snRNA molecule to identify proteins associated with U7 snRNP/U7 snRNA that could be potentially involved in core histone genes expression in human cells. Mass spectrometric analysis of affinity-purified fraction revealed, among others, multifunctional RNA/DNAbinding protein FUS/TLS (fused in sarcoma/translocated in liposarcoma) as a new factor interacting with U7 snRNA/RNP. Co-immunoprecipitation and RIP experiments confirmed the binding between FUS and the U7 RNA/snRNP.
Interestingly, FUS:U7 snRNA interaction seems to be activated in S phase where the core histone genes are expressed. Moreover, FUS co-fractionates in 10-50% continuous glycerol gradient with other factors involved in histone premRNAs 3’end processing. However, this unique 3’end maturation was not disturbed upon FUS knockdown. Instead, we found that FUS depletion leads to a de-regulation of expression from selected histone promoters, suggesting that FUS is rather involved in regulation of core histone genes transcription. Thus, FUS bound to U7 snRNP can play a role in coupling between transcription and 3’end processing of replication dependant histone mRNAs.
Item Type: |
Conference or Workshop Item (Poster) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) |
UniBE Contributor: |
Ruepp, Marc-David |
Subjects: |
500 Science > 570 Life sciences; biology 500 Science > 540 Chemistry |
Language: |
English |
Submitter: |
Christina Schüpbach |
Date Deposited: |
05 Aug 2014 14:30 |
Last Modified: |
05 Dec 2022 14:36 |
URI: |
https://boris.unibe.ch/id/eprint/57533 |
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