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Akademický článek

A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing

Autor: Sunbin Liu, Sina Mozaffari-Jovin, Jan Wollenhaupt, Karine F Santos, Matthias Theuser, Stanislaw Dunin-Horkawicz, Patrizia Fabrizio, Janusz M Bujnicki, Reinhard Lührmann, Markus C Wahl

Publikováno v: eLife, Vol 4 (2015)

Prp3 is an essential U4/U6 di-snRNP-associated protein whose functions and molecular mechanisms in pre-mRNA splicing are presently poorly understood. We show by structural and biochemical analyses that Prp3 contains a bipartite U4/U6 di-snRNA-binding

Externí odkaz: https://doaj.org/article/3b0881cfdd874157b3987c784fcd7a22

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A skipping rope translocation mechanism in a widespread family of DNA repair helicases

Autor: Markus C. Wahl, Johann J Roske, Sunbin Liu, Bernhard Loll, Ursula Neu

Publikováno v: Nucleic acids research 49(1), 504-518 (2020). doi:10.1093/nar/gkaa1174
Nucleic Acids Research

Nucleic acids research / Special publication 49(1), 504 - 518 (2021). doi:10.1093/nar/gkaa1174
Mitomycin repair factor A represents a family of DNA helicases that harbor a domain of unknown function (DUF1998) and support repair of mitomycin C-in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d00c46fea068acc1ea840b08029156ba
https://bib-pubdb1.desy.de/record/474991

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RIM binding protein couples synaptic vesicle recruitment to release sites

Publikováno v: The Journal of Cell Biology
The journal of cell biology 219(7), e201902059 (2020). doi:10.1083/jcb.201902059

Petzoldt et al. investigate the functional protein architecture at the presynaptic active zone, an elaborate protein scaffold organizing synaptic vesicle (SV) release. They find that the conserved multidomain protein RIM-BP provides a relay to guide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::948e8ac8657ae792620e23b748e81ed2
http://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=102723

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Akademický článek

Binding of the Human Prp31 Nop Domain to a Composite RNA-Protein Platform in U4 snRNP.

Autor: Sunbin Liu¹, Ping Li^1,2, Dybkov, Olexandr¹, Nottrott, Stephanie¹, Hartmuth, Klaus¹, Lührmann, Reinhard¹ Reinhard.Luehrmann@mpi-bpc.mpg.de, Carlomagno, Teresa² taco@nmr.mpibpc.mpg.de, Wahl, Markus C.³ mwahL@gwdg.de

Publikováno v: Science. 4/6/2007, Vol. 316 Issue 5821, p115-120. 6p. 4 Diagrams.

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Structure determination by multiple-wavelength anomalous dispersion (MAD) at the Pr LIIIedge

Autor: Uwe Mueller, Michael Hellmig, Sandra Puehringer, Manfred S. Weiss, Markus C. Wahl, Sunbin Liu

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68:981-984

The use of longer X-ray wavelengths in macromolecular crystallography has grown significantly over the past few years. The main reason for this increased use of longer wavelengths has been to utilize the anomalous signal from sulfur, providing a mean

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e0acde5ffe22998937998f0ca585609
https://doi.org/10.1107/s1744309112025456

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Binding of the Human Prp31 Nop Domain to a Composite RNA-Protein Platform in U4 snRNP

Autor: Stephanie Nottrott, Teresa Carlomagno, Klaus Hartmuth, Olexandr Dybkov, Reinhard Lührmann, Ping Li, Markus C. Wahl, Sunbin Liu

Publikováno v: Science

Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nucle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2109764a199ee9caabb62e7856b7181
https://doi.org/10.1126/science.1137924

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Structure of a Multipartite Protein-Protein Interaction Domain in Splicing Factor Prp8 and Its Link to Retinitis Pigmentosa

Autor: Markus C. Wahl, Reinhard Lührmann, Janusz M. Bujnicki, Sunbin Liu, Vladimir Pena

Publikováno v: Molecular Cell

Protein Prp8 interacts with several other spliceosomal proteins, snRNAs, and the pre-mRNA and thereby organizes the active site(s) of the spliceosome. The DEAD-box protein Brr2 and the GTPase Snu114 bind to the Prp8 C terminus, a region where mutatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1db5e31747f2e0564ee5635a0f4e772c

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A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing

Autor: Janusz M. Bujnicki, Patrizia Fabrizio, Reinhard Lührmann, Karine F. Santos, Matthias Theuser, Jan Wollenhaupt, Sina Mozaffari-Jovin, Markus C. Wahl, Sunbin Liu, Stanislaw Dunin-Horkawicz

Publikováno v: eLife, Vol 4 (2015)
eLife

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d0223fcc7f58fea22c60a40bdc2f986
https://elifesciences.org/articles/07320

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Structural basis for the dual U4 and U4atac snRNA-binding specificity of spliceosomal protein hPrp31

Autor: Homa Ghalei, Reinhard Lührmann, Markus C. Wahl, Sunbin Liu

Publikováno v: RNA

Human proteins 15.5K and hPrp31 are components of the major spliceosomal U4 snRNP and of the minor spliceosomal U4atac snRNP. The two proteins bind to related 5′-stem loops (5′SLs) of the U4 and U4atac snRNAs in a strictly sequential fashion. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6039cbf495fc252ab8fc612211409ab9
https://hdl.handle.net/11858/00-001M-0000-0027-C6B6-F11858/00-001M-0000-000F-0191-211858/00-001M-0000-0027-C6B5-2

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