FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors.

Raczynska, Katarzyna Dorota; Ruepp, Marc-David; Brzek, Aleksandra; Reber, Stefan; Romeo, Valentina; Rindlisbacher, Barbara; Heller, Manfred; Szweykowska-Kulinska, Zofia; Jarmolowski, Artur; Schümperli, Daniel (2015). FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors. Nucleic acids research, 43(20), pp. 9711-9728. Oxford University Press 10.1093/nar/gkv794

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Replication-dependent histone genes are up-regulated during the G1/S phase transition to meet the requirement for histones to package the newly synthesized DNA. In mammalian cells, this increment is achieved by enhanced transcription and 3' end processing. The non-polyadenylated histone mRNA 3' ends are generated by a unique mechanism involving the U7 small ribonucleoprotein (U7 snRNP). By using affinity purification methods to enrich U7 snRNA, we identified FUS/TLS as a novel U7 snRNP interacting protein. Both U7 snRNA and histone transcripts can be precipitated by FUS antibodies predominantly in the S phase of the cell cycle. Moreover, FUS depletion leads to decreased levels of correctly processed histone mRNAs and increased levels of extended transcripts. Interestingly, FUS antibodies also co-immunoprecipitate histone transcriptional activator NPAT and transcriptional repressor hnRNP UL1 in different phases of the cell cycle. We further show that FUS binds to histone genes in S phase, promotes the recruitment of RNA polymerase II and is important for the activity of histone gene promoters. Thus, FUS may serve as a linking factor that positively regulates histone gene transcription and 3' end processing by interacting with the U7 snRNP and other factors involved in replication-dependent histone gene expression.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Cell Biology
04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DCR Services > Core Facility Massenspektrometrie- und Proteomics-Labor
04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Institute of Clinical Chemistry
08 Faculty of Science > Departement of Chemistry and Biochemistry
08 Faculty of Science > Department of Biology > Institute of Cell Biology > RNA

Graduate School:

Graduate School for Cellular and Biomedical Sciences (GCB)

UniBE Contributor:

Ruepp, Marc-David; Reber, Stefan; Romeo, Valentina; Büchel, Barbara; Heller, Manfred and Schümperli, Daniel

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health
500 Science > 540 Chemistry
500 Science

ISSN:

0305-1048

Publisher:

Oxford University Press

Language:

English

Submitter:

Daniel Schümperli

Date Deposited:

11 Feb 2016 16:28

Last Modified:

16 Nov 2018 02:30

Publisher DOI:

10.1093/nar/gkv794

PubMed ID:

26250115

BORIS DOI:

10.7892/boris.71618

URI:

https://boris.unibe.ch/id/eprint/71618

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