Quantitative global studies reveal differential translational control by start codon context across the fungal kingdom

Autor: Frédérique Moyrand, Prashanthi Natarajan, Guilhem Janbon, Jade Sales-Lee, Laura R. Tuck, Frank Feuerbach, Wallace Ewj, Luciana de Oliveira, Hiten D. Madhani, Corinne Maufrais

Publikováno v: Wallace, E W J, Maufrais, C, Sales Lee, J, Tuck, L, de Oliveira, L, Feuerbach, F, Moyrand, F, Natarajan, P, Madhani, H D & Janbon, G 2020, ' Quantitative global studies reveal differential translational control by start codon context across the fungal kingdom ', Nucleic Acids Research, vol. 48, no. 5, pp. 2312-2331 . https://doi.org/10.1093/nar/gkaa060
Nucleic Acids Research
Nucleic Acids Research, 2020, 48 (5), pp.2312-2331. ⟨10.1093/nar/gkaa060⟩
Nucleic Acids Research, Oxford University Press, 2020, 48 (5), pp.2312-2331. ⟨10.1093/nar/gkaa060⟩

Eukaryotic protein synthesis generally initiates at a start codon defined by an AUG and its surrounding Kozak sequence context, but the quantitative importance of this context in different species is unclear. We tested this concept in two pathogenic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf61a7e41b710769c98f2c49ddc7d2bf
https://www.pure.ed.ac.uk/ws/files/133847580/gkaa060.pdf

eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition

Autor: Adeline Renaud, A. Myasnikov, Lauriane Kuhn, Angelita Simonetti, Yaser Hashem, Jailson Brito Querido, Eder Mancera-Martínez

Publikováno v: Molecular Cell
Molecular Cell, 2016, 63 (2), pp.206-217. ⟨10.1016/j.molcel.2016.05.033⟩
Molecular Cell, Elsevier, 2016, 63 (2), pp.206-217. ⟨10.1016/j.molcel.2016.05.033⟩

International audience; mRNA translation initiation in eukaryotes requires the cooperation of a dozen eukaryotic initiation factors (eIFs) forming several complexes, which leads to mRNA attachment to the small ribosomal 40S subunit, mRNA scanning for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d5b377195d9c0e3791d3c992cbf2e74
https://hal.science/hal-02294734

Hierarchical subfunctionalization of fabp1a, fabp1b and fabp10 tissue-specific expression may account for retention of these duplicated genes in the zebrafish (Danio rerio) genome

Autor: Jonathan M. Wright, Bernard Thisse, Rong-Zong Liu, Eileen M. Denovan-Wright, Mukesh K. Sharma, Christine Thisse

Publikováno v: FEBS Journal
FEBS Journal, Wiley, 2006, 273 (14), pp.3216-29. ⟨10.1111/j.1742-4658.2006.05330.x⟩

International audience; Fatty acid-binding protein type 1 (FABP1), commonly termed liver-type fatty acid-binding protein (L-FABP), is encoded by a single gene in mammals. We cloned and sequenced cDNAs for two distinct FABP1s in zebrafish coded by gen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e08b900db8df2baae85152231ce867d
https://doi.org/10.1111/j.1742-4658.2006.05330.x

The control ofAzorhizobium caulinodans nifAexpression by oxygen, ammonia and by the HF‐I‐like protein, NrfA

Autor: Pierre Alexandre Kaminski, Claudine Elmerich

Publikováno v: Molecular Microbiology
Molecular Microbiology, 1998, 28 (3), pp.603-613. ⟨10.1046/j.1365-2958.1998.00823.x⟩

International audience; The control of Azorhizobium caulinodans nifA expression in response to oxygen and ammonia involves FixLJ, FixK, NtrBC, NtrXY and the HF-I-like protein NrfA. The regulation is thus complex and possibly involves post-transcripti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67553d862fa5fdd1928b470852c533c9
https://doi.org/10.1046/j.1365-2958.1998.00823.x

The Indispensable N-Terminal Half of eIF3j/HCR1 Cooperates with its Structurally Conserved Binding Partner eIF3b/PRT1-RRM and with eIF1A in Stringent AUG Selection

Autor: Susan Wagner, Edit Rutkai, Martina Karásková, Peter J. Lukavsky, Leoš Shivaya Valášek, Anna Herrmannová, Latifa ElAntak

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, 2010, 396 (4), pp.1097-1116. ⟨10.1016/j.jmb.2009.12.047⟩
Journal of Molecular Biology, Elsevier, 2010, 396 (4), pp.1097-1116. ⟨10.1016/j.jmb.2009.12.047⟩
Journal of Molecular Biology, Elsevier, 2010, 396 (4), pp.1097-116. ⟨10.1016/j.jmb.2009.12.047⟩
Journal of molecular biology

International audience; Despite recent progress in our understanding of the numerous functions of individual subunits of eukaryotic translation initiation factor (eIF) 3, little is known on the molecular level. Using NMR spectroscopy, we determined t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd38e533051113739f8fb98abfd532b1
https://hal.science/hal-02018169/file/JMolBiol2010.pdf