Affinity proteomic dissection of the human nuclear cap-binding complex interactome
| Autor: | Mehrnoosh Oghbaie, Ilya Altukhov, Torben Heick Jensen, Maria Pashkova, Michael P. Rout, Svetlana Kalmykova, Hua Jiang, Brian T. Chait, David Fenyö, Yuhui Dou, Kelly R. Molloy, John LaCava |
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| Přispěvatelé: | Damage and Repair in Cancer Development and Cancer Treatment (DARE) |
| Rok vydání: | 2020 |
| Předmět: |
Proteomics
RNA Caps Cytoplasm COMPUTATIONAL PLATFORM Proteome AcademicSubjects/SCI00010 RNA EXPORT PROTEINS Exosome complex SPLICEOSOME Context (language use) Computational biology Biology Interactome Exosome EXPLORATION Narese/16 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine RNA polymerase Genetics RNA and RNA-protein complexes CRYO-EM STRUCTURE Humans Nuclear Cap-Binding Protein Complex 030304 developmental biology Ribonucleoprotein Messenger RNA 0303 health sciences PURIFICATION Cap binding complex Exosome Multienzyme Ribonuclease Complex IDENTIFICATION Chemistry Nuclear Proteins RNA MASS-SPECTROMETRY RNA Cap-Binding Proteins RNA Polymerase II MESSENGER-RNA 030217 neurology & neurosurgery CBC |
| Zdroj: | Nucleic Acids Research, 48(18), 10456-10469. Oxford University Press Nucleic Acids Research Dou, Y, Kalmykova, S, Pashkova, M, Oghbaie, M, Jiang, H, Molloy, K R, Chait, B T, Rout, M P, Fenyö, D, Jensen, T H, Altukhov, I & LaCava, J 2020, ' Affinity proteomic dissection of the human nuclear cap-binding complex interactome ', Nucleic Acids Research, vol. 48, no. 18, pp. 10456-10469 . https://doi.org/10.1093/nar/gkaa743 |
| ISSN: | 0305-1048 |
| Popis: | A 5’, 7-methylguanosine cap is a quintessential feature of RNA polymerase II-transcribed RNAs, and a textbook aspect of co-transcriptional RNA processing. The cap is bound by the cap-binding complex (CBC), canonically consisting of nuclear cap-binding proteins 1 and 2 (NCBP1/2). The CBC has come under renewed investigative interest in recent years due to its participation in RNA-fate decisions via interactions with RNA productive factors as well as with adapters of the degradative RNA exosome - including the proteins SRRT (a.k.a. ARS2) and ZC3H18, and macromolecular assemblies such as the nuclear exosome targeting (NEXT) complex and the poly(A) exosome targeting (PAXT) connection. A novel cap-binding protein, NCBP3, was recently proposed to form an alternative, non-canonical CBC together with NCBP1, and to interact with the canonical CBC along with the protein SRRT. The theme of post-transcriptional RNA fate, and how it relates to co-transcriptional ribonucleoprotein assembly is abundant with complicated, ambiguous, and likely incomplete models. In an effort to clarify the compositions of NCBP1-, 2-, and 3-related macromolecular assemblies, including their intersections and differences, we have applied an affinity capture-based interactome screening approach, where the experimental design and data processing have been modified and updated to identify interactome differences between targets under a range of experimental conditions, in the context of label-free quantitative mass spectrometry. This study generated a comprehensive view of NCBP-protein interactions in the ribonucleoprotein context and demonstrates the potential of our approach to benefit the interpretation of complex biological pathways. |
| Databáze: | OpenAIRE |
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