Výsledky vyhledávání - "RNA/chemistry/*metabolism"

Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain

Autor: Bertrand Séraphin, Benedetta Sposito, Chris Oubridge, Kiyoshi Nagai, Eiji Obayashi, Anne-Marie M. van Roon, Andrew J. Newman

Publikováno v: 'RNA ', vol: 23, pages: 968-981 (2017)
RNA
RNA, Cold Spring Harbor Laboratory Press, 2017, 23 (6), pp.968-981. ⟨10.1261/rna.059378.116⟩

Spliceosomal proteins Hsh49p and Cus1p are components of SF3b, which together with SF3a, Msl1p/Lea1p, Sm proteins, and U2 snRNA, form U2 snRNP, which plays a crucial role in pre-mRNA splicing. Hsh49p, comprising two RRMs, forms a heterodimer with Cus

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cb4599ebeb50b190511b6438430c06d
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:47208

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An artificial PPR scaffold for programmable RNA recognition

Autor: Aleksandra Filipovska, Oliver Rackham, Tiongsun Chia, Muhammad Fazril Mohamad Razif, Lional Rajappa, Stéphane Thore, James P. Lingford, Sandrine Claire Coquille

Publikováno v: Nature Communications, Vol. 5 (2014) P. 5729

Pentatricopeptide repeat (PPR) proteins control diverse aspects of RNA metabolism in eukaryotic cells. Although recent computational and structural studies have provided insights into RNA recognition by PPR proteins, their highly insoluble nature and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a89d94ca7401147dde92781d26290630
https://pubmed.ncbi.nlm.nih.gov/25517350

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Structure and assembly of the Alu domain of the mammalian signal recognition particle

Autor: Klemens Wild, Stephen Cusack, Oliver Weichenrieder, Katharina Strub

Publikováno v: Nature, Vol. 408, No 6809 (2000) pp. 167-73

The Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. It retards the ribosomal elongation of signal-peptide-containing proteins bef

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3991f548ff1ffb572de6d57060e591f0
https://doi.org/10.1038/35041507

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Hierarchical assembly of the Alu domain of the mammalian signal recognition particle

Autor: Katharina Strub, Oliver Weichenrieder, Stephen Cusack, Darcy E.A. Birse, Catherine Stehlin, Peter A. Timmins, Ulrike Kapp

Publikováno v: RNA, Vol. 7, No 5 (2001) pp. 731-40

The mammalian signal recognition particle (SRP) catalytically promotes cotranslational translocation of signal sequence containing proteins across the endoplasmic reticulum membrane. While the S-domain of SRP binds the N-terminal signal sequence on t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a410bf79ccb96777e9fc07c98003612a
https://pubmed.ncbi.nlm.nih.gov/11350037

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Identification of a minimal Alu RNA folding domain that specifically binds SRP9/14

Autor: Weichenrieder O, Kapp U, Stephen Cusack, Strub K

Publikováno v: RNA: A Publication of the RNA Society
Europe PubMed Central
RNA, Vol. 3, No 11 (1997) pp. 1262-74
EMBL-EBI

We have identified functionally and analyzed a minimal Alu RNA folding domain that is recognized by SRPphi14-9. Recombinant SRPphi14-9 is a fusion protein containing on a single polypeptide chain the sequences of both the SRP14 and SRP9 proteins that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::70bf05f852c4f881452e39128d808fcb
https://hdl.handle.net/21.11116/0000-000C-9001-F

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Mutational analysis of the protein subunits of the signal recognition particle Alu-domain

Autor: Bui, Nazarena, Wolff, N, Cusack, S, Strub, Katharina

Publikováno v: RNA, Vol. 3, No 7 (1997) pp. 748-63

Two polypeptides of the murine signal recognition particle (SRP), SRP9 and SRP14, bind exclusively as a heterodimer to SRP RNA and their presence is required for elongation arrest activity of the particle. SRP9/14 also constitute a subunit of small c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::b95a15ababdcf1508e2d92a9b9620fff
https://europepmc.org/articles/PMC1369522/

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The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14

Autor: Stephen Cusack, Darcy E.A. Birse, Anders E Åberg, Katharina Strub, Ulrike Kapp

Publikováno v: EMBO Journal, Vol. 16, No 13 (1997) pp. 3757-66

The mammalian signal recognition particle (SRP) is an 11S cytoplasmic ribonucleoprotein that plays an essential role in protein sorting. SRP recognizes the signal sequence of the nascent polypeptide chain emerging from the ribosome, and targets the r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f311b933cdb4e8dadb48aac95f420e97
https://europepmc.org/articles/PMC1169999/

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