日本語
 
Help Privacy Policy ポリシー/免責事項
  詳細検索ブラウズ

アイテム詳細


公開

学術論文

CAPRI enables comparison of evolutionary conserved RNA interacting regions

MPS-Authors

Panhale,  Amol
Department of Chromatin Regulation, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Richter ,  Florian M.
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

/persons/resource/persons241977

Ramírez,  Fidel
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Shvedunova,  Maria
Department of Chromatin Regulation, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

/persons/resource/persons50420

Manke,  Thomas
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

/persons/resource/persons191219

Mittler,  Gerhard
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

/persons/resource/persons198888

Akhtar,  Asifa
Department of Chromatin Regulation, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

External Resource
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
フルテキスト (公開)
公開されているフルテキストはありません
付随資料 (公開)
There is no public supplementary material available
引用

Panhale, A., Richter, F. M., Ramírez, F., Shvedunova, M., Manke, T., Mittler, G., & Akhtar, A. (2019). CAPRI enables comparison of evolutionary conserved RNA interacting regions. Nature Communications, 10:. doi:10.1038/s41467-019-10585-3.


引用: https://hdl.handle.net/21.11116/0000-0004-E442-0
要旨
RNA-protein complexes play essential regulatory roles at nearly all levels of gene expression. Using in vivo crosslinking and RNA capture, we report a comprehensive RNA-protein interactome in a metazoan at four levels of resolution: single amino acids, domains, proteins and multisubunit complexes. We devise CAPRI, a method to map RNA-binding domains (RBDs) by simultaneous identification of RNA interacting crosslinked peptides and peptides adjacent to such crosslinked sites. CAPRI identifies more than 3000 RNA proximal peptides in Drosophila and human proteins with more than 45% of them forming new interaction interfaces. The comparison of orthologous proteins enables the identification of evolutionary conserved RBDs in globular domains and intrinsically disordered regions (IDRs). By comparing the sequences of IDRs through evolution, we classify them based on the type of motif, accumulation of tandem repeats, conservation of amino acid composition and high sequence divergence.