Available to mentor
Jay Brito Querido obtained his B.S. in biochemistry and M.Sc. in medical biochemistry from the University of Lisbon, Portugal, followed by a Ph.D. in cellular and molecular biology at the University of Strasbourg, France. In 2018, he started his postdoc at the MRC Laboratory of Molecular Biology (United Kingdom) in the laboratory of Dr. Venki Ramakrishnan.
Jay has been named RNA Faculty Scholar by the Center for RNA Biomedicine, a Biological Sciences Scholar by the University of Michigan Medical School, and a member of the University of Michigan Rogel Cancer Center.
Lab Website twitter
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Postdoctoral ScientistMRC Laboratory of Molecular Biology, Cambridge, 2022
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Postdoctoral Research AssociateUniversity of Cambridge, Clare Hall College, 2022
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Center MemberRogel Cancer Center
The regulation of mRNA translation into protein is fundamental for life. Translation is controlled mainly during its initiation stage. Our lab uses cryo-electron microscopy in combination with biochemical and genetic approaches to study the role of a family of enzymes called DEAD-box (DDX) RNA helicases in the regulation of translation initiation, and how this initiation is regulated in health and disease.
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Brito Querido J, Sokabe M, Díaz-López I, Gordiyenko Y, Zuber P, Du Y, Albacete-Albacete L, Ramakrishnan V, Fraser CS. Nat Commun, 2024 Aug 8; 15 (1): 6633Journal ArticleHuman tumor suppressor protein Pdcd4 binds at the mRNA entry channel in the 40S small ribosomal subunit.
DOI:10.1038/s41467-024-50672-8 PMID: 39117603 -
Wang F, Holmes MJ, Hong HJ, Thaprawat P, Kannan G, Huynh M-H, Schultz TL, Licon MH, Lourido S, Dong W, Brito Querido J, Sullivan WJ, O'Leary SE, Carruthers VB. Nat Commun, 2024 May 23; 15 (1): 4385Journal ArticleTranslation initiation factor eIF1.2 promotes Toxoplasma stage conversion by regulating levels of key differentiation factors.
DOI:10.1038/s41467-024-48685-4 PMID: 38782906 -
Brito Querido J, Díaz-López I, Ramakrishnan V. Nat Rev Mol Cell Biol, 2024 Mar; 25 (3): 168 - 186.Journal ArticleThe molecular basis of translation initiation and its regulation in eukaryotes.
DOI:10.1038/s41580-023-00624-9 PMID: 38052923 -
Brito Querido J, Sokabe M, Díaz-López I, Gordiyenko Y, Fraser CS, Ramakrishnan V. Nat Struct Mol Biol, 2024 Mar; 31 (3): 455 - 464.Journal ArticleThe structure of a human translation initiation complex reveals two independent roles for the helicase eIF4A.
DOI:10.1038/s41594-023-01196-0 PMID: 38287194 -
Bochler A, Querido JB, Prilepskaja T, Soufari H, Simonetti A, Del Cistia ML, Kuhn L, Ribeiro AR, Valášek LS, Hashem Y. Cell Rep, 2020 Dec 22; 33 (12): 108534Journal ArticleStructural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.
DOI:10.1016/j.celrep.2020.108534 PMID: 33357443 -
Brito Querido J, Sokabe M, Kraatz S, Gordiyenko Y, Skehel JM, Fraser CS, Ramakrishnan V. Science, 2020 Sep 4; 369 (6508): 1220 - 1227.Journal ArticleStructure of a human 48S translational initiation complex.
DOI:10.1126/science.aba4904 PMID: 32883864 -
Brito Querido J, Mancera-Martínez E, Vicens Q, Bochler A, Chicher J, Simonetti A, Hashem Y. Structure, 2017 Dec 5; 25 (12): 1785 - 1794.e3.Journal ArticleThe cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein.
DOI:10.1016/j.str.2017.09.014 PMID: 29107485 -
Simonetti A, Brito Querido J, Myasnikov AG, Mancera-Martinez E, Renaud A, Kuhn L, Hashem Y. Mol Cell, 2016 Jul 21; 63 (2): 206 - 217.Journal ArticleeIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition.
DOI:10.1016/j.molcel.2016.05.033 PMID: 27373335
