Proteomics

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Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker


ABSTRACT: To identify components of the U7 snRNP, we used cleavage-resistant histone pre-mRNA containing biotin and a photo-sensitive linker and purify processing complexes from Drosophila and mouse nuclear extracts.

INSTRUMENT(S): LTQ Orbitrap Velos, LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Drosophila Melanogaster (fruit Fly) Mus Musculus (mouse)

SUBMITTER: Aleksandra Skrajna  

LAB HEAD: Michał Dadlez

PROVIDER: PXD008917 | Pride | 2018-03-08

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
50430skra_gel_1.mgf Mgf
50430skra_gel_1.mzid Mzid
50430skra_gel_1.raw Raw
50430skra_gel_2.mgf Mgf
50430skra_gel_2.mzid Mzid
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Publications

Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker.

Skrajna Aleksandra A   Yang Xiao-Cui XC   Dadlez Michal M   Marzluff William F WF   Dominski Zbigniew Z  

Nucleic acids research 20180501 9


3' end cleavage of metazoan replication-dependent histone pre-mRNAs requires the multi-subunit holo-U7 snRNP and the stem-loop binding protein (SLBP). The exact composition of the U7 snRNP and details of SLBP function in processing remain unclear. To identify components of the U7 snRNP in an unbiased manner, we developed a novel approach for purifying processing complexes from Drosophila and mouse nuclear extracts. In this method, catalytically active processing complexes are assembled in vitro  ...[more]

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