NMR solution structure determination of large RNA-protein complexes

Autor: Deepak Kumar Yadav, Peter J. Lukavsky

Publikováno v: Progress in Nuclear Magnetic Resonance Spectroscopy. 97:57-81

Structure determination of RNA-protein complexes is essential for our understanding of the multiple layers of RNA-mediated posttranscriptional regulation of gene expression. Over the past 20years, NMR spectroscopy became a key tool for structural stu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::190c39495d0606678171b79a6fc64c22
https://doi.org/10.1016/j.pnmrs.2016.10.001

The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity

Autor: Christine von Schroetter, Antoine Cléry, Peter J. Lukavsky, Magdalini Polymenidou, Eva Maria Hock, Oliver Mühlemann, Tamara Kazeeva, Marc-David Ruepp, Fionna E. Loughlin, Frédéric H.-T. Allain, Martino Colombo, Stefan Reber, Phillip Pauli

Publikováno v: Molecular Cell
Loughlin, F E, Lukavsky, P J, Kazeeva, T, Reber, S, Hock, E-M, Colombo, M, Von Schroetter, C, Pauli, P, Cléry, A, Mühlemann, O, Polymenidou, M, Ruepp, M-D & Allain, F H-T 2019, ' The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity ', MOLECULAR CELL, vol. 73, no. 3, pp. 490-504.e6 . https://doi.org/10.1016/j.molcel.2018.11.012

Fused in sarcoma (FUS) is an RNA binding protein involved in regulating many aspects of RNA process- ing and linked to several neurodegenerative dis- eases. Transcriptomics studies indicate that FUS binds a large variety of RNA motifs, suggesting tha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b8cafed56772759efbc4a8da27ed658
https://pubmed.ncbi.nlm.nih.gov/30581145

Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly

Autor: Dalia Daujotytė, Peter J. Lukavsky, Leoš Shivaya Valášek, Ji-Chun Yang, Fabrice Gorrec, Lucie Cuchalová, Anna Herrmannová, István Dányi, Susan Wagner

Publikováno v: Nucleic Acids Research

Translation initiation factor eIF3 acts as the key orchestrator of the canonical initiation pathway in eukaryotes, yet its structure is greatly unexplored. We report the 2.2 A resolution crystal structure of the complex between the yeast seven-bladed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8d08715bf36c626cdd78237eabd7bc9
http://europepmc.org/articles/PMC3300007

Conserved functional domains and a novel tertiary interaction near the pseudoknot drive translational activity of hepatitis C virus and hepatitis C virus-like internal ribosome entry sites

Autor: Laura E. Easton, Peter J. Lukavsky, Nicolas Locker

Publikováno v: Nucleic Acids Research

The translational activity of the hepatitis C virus (HCV) internal ribosome entry site (IRES) and other HCV-like IRES RNAs depends on structured RNA elements in domains II and III, which serve to recruit the ribosomal 40S subunit, eukaryotic initiati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14c3b31b35691e6f71f700bd2e1bb921
https://doi.org/10.1093/nar/gkp588

Affinity purification of eukaryotic 48S initiation complexes

Autor: Nicolas Locker, Laura E. Easton, Peter J. Lukavsky

Publikováno v: RNA. 12:683-690

In vitro assembly of translation initiation complexes from higher eukaryotes requires purification of ribosomal subunits, eukaryotic initiation factors, and initiator tRNA from natural sources, and therefore yields only limited material for functiona

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef1c67450674f0c86d9e861bfbf2f37f
https://doi.org/10.1261/rna.2227906