دورية أكاديمية
Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during $\mathrm{3^{\prime}}$-splice site recognition
| العنوان: | Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during $\mathrm{3^{\prime}}$-splice site recognition |
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| المؤلفون: | Zhang, Y., Madl, T., Bagdiul, I., Kern, T., Kang, H.-S., Zou, P., Maeusbacher, N., Sieber, S. A., Kraemer, A., Sattler, M. |
| المصدر: | Nucleic acids research 41(2), 1343-1354 (2012). doi:10.1093/nar/gks1097 |
| بيانات النشر: | Information Retrieval Ltd. |
| سنة النشر: | 2012 |
| المجموعة: | DESY Publication Database (PUBDB) |
| مصطلحات موضوعية: | info:eu-repo/classification/ddc/540, Amino Acid Sequence, DNA-Binding Proteins: chemistry, DNA-Binding Proteins: metabolism, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins: chemistry, Nuclear Proteins: metabolism, Phosphorylation, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Secondary, RNA: metabolism, RNA Splice Sites, Ribonucleoproteins: chemistry, Ribonucleoproteins: metabolism, Sequence Homology, Amino Acid, Serine: metabolism, Transcription Factors: chemistry, Transcription Factors: metabolism, DNA-Binding Proteins, Nuclear Proteins, Ribonucleoproteins, SF1 protein, human, Transcription Factors |
| جغرافية الموضوع: | DE |
| الوصف: | Recognition of the 3'-splice site is a key step in pre-mRNA splicing and accomplished by a dynamic complex comprising splicing factor 1 (SF1) and the U2 snRNP auxiliary factor 65-kDa subunit (U2AF65). Both proteins mediate protein-protein and protein-RNA interactions for cooperative RNA-binding during spliceosome assembly. Here, we report the solution structure of a novel helix-hairpin domain in the N-terminal region of SF1 (SF1(NTD)). The nuclear magnetic resonance- and small-angle X-ray scattering-derived structure of a complex of the SF1(NTD) with the C-terminal U2AF homology motif domain of U2AF65 (U2AF65(UHM)) reveals that, in addition to the known U2AF65(UHM)-SF1 interaction, the helix-hairpin domain forms a secondary, hydrophobic interface with U2AF65(UHM), which locks the orientation of the two subunits. Mutational analysis shows that the helix hairpin is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. We further show that tandem serine phosphorylation of a conserved Ser80-Pro81-Ser82-Pro83 motif rigidifies a long unstructured linker in the SF1 helix hairpin. Phosphorylation does not significantly alter the overall conformations of SF1, SF1-U2AF65 or the SF1-U2AF65-RNA complexes, but slightly enhances RNA binding. Our results indicate that the helix-hairpin domain of SF1 is required for cooperative 3'-splice site recognition presumably by stabilizing a unique quaternary arrangement of the SF1-U2AF65-RNA complex. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/wos/WOS:000314121100060; info:eu-repo/semantics/altIdentifier/issn/1362-4962; info:eu-repo/semantics/altIdentifier/pmid/pmid:23175611; https://bib-pubdb1.desy.de/record/142643Test; https://bib-pubdb1.desy.de/search?p=id:%22PHPPUBDB-25603%22Test |
| الإتاحة: | https://doi.org/10.1093/nar/gks1097Test https://doi.org/10.3204/PHPPUBDB-25603Test https://bib-pubdb1.desy.de/record/142643Test https://bib-pubdb1.desy.de/search?p=id:%22PHPPUBDB-25603%22Test |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.5CC5661D |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |