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  A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity.

Boesler, C., Rigo, N., Anokhina, M. M., Tauchert, M. J., Agafonov, D. E., Kastner, B., et al. (2016). A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity. Nature Communications, 7: 11997. doi:10.1038/ncomms11997.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-24E8-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-24F0-E
Genre: Journal Article

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 Creators:
Boesler, C.1, Author              
Rigo, N.1, Author              
Anokhina, M. M.1, Author              
Tauchert, M. J., Author
Agafonov, D. E.1, Author              
Kastner, B.1, Author              
Urlaub, H.2, Author              
Ficner, R., Author
Will, C. L.1, Author              
Lührmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578576              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: The precise role of the spliceosomal DEAD-box protein Prp28 in higher eukaryotes remains unclear. We show that stable tri-snRNP association during pre-catalytic spliceosomal B complex formation is blocked by a dominant-negative hPrp28 mutant lacking ATPase activity. Complexes formed in the presence of ATPase-deficient hPrp28 represent a novel assembly intermediate, the pre-B complex, that contains U1, U2 and loosely associated tri-snRNP and is stalled before disruption of the U1/5'ss base pairing interaction, consistent with a role for hPrp28 in the latter. Pre-B and B complexes differ structurally, indicating that stable tri-snRNP integration is accompanied by substantial rearrangements in the spliceosome. Disruption of the U1/5'ss interaction alone is not sufficient to bypass the block by ATPase-deficient hPrp28, suggesting hPrp28 has an additional function at this stage of splicing. Our data provide new insights into the function of Prp28 in higher eukaryotes, and the requirements for stable tri-snRNP binding during B complex formation.

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Language(s): eng - English
 Dates: 2016-07-05
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms11997
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Title: Nature Communications
Source Genre: Journal
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Pages: 12 Volume / Issue: 7 Sequence Number: 11997 Start / End Page: - Identifier: -