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pro vyhledávání: '"Charles T. Lauhon"'
Autor:
Charles Cirio, Herman van Tilbeurgh, Mark G Fulton, Charles T. Lauhon, S. Missoury, Brett J. Kopina, Bruno Collinet
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2021, ⟨10.1093/nar/gkab026⟩
Nucleic Acids Research, Oxford University Press, 2021, ⟨10.1093/nar/gkab026⟩
Nucleic Acids Research, 2021, ⟨10.1093/nar/gkab026⟩
Nucleic Acids Research, Oxford University Press, 2021, ⟨10.1093/nar/gkab026⟩
The tRNA modification N6-threonylcarbamoyladenosine (t6A) is universally conserved in all organisms. In bacteria, the biosynthesis of t6A requires four proteins (TsaBCDE) that catalyze the formation of t6A via the unstable intermediate l-threonylcarb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c25be9170c566e6d516fe181b3752133
https://hal.sorbonne-universite.fr/hal-03134410
https://hal.sorbonne-universite.fr/hal-03134410
Autor:
Charles T. Lauhon
In bacteria, tRNAs that decode 4-fold degenerate family codons and have uridine at position 34 of the anticodon are typically modified with either 5-methoxyuridine (mo(5)U) or 5-methoxycarbonylmethoxyuridine (mcmo(5)U). These modifications are critic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2219ed85804c2e146749777c599e1291
https://europepmc.org/articles/PMC6755726/
https://europepmc.org/articles/PMC6755726/
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:421-424
The sulfurtransferase 4-thiouridine synthetase (ThiI) is involved in the ATP-dependent modification of U8 in tRNA. ThiI fromThermotoga maritimawas cloned, overexpressed and purified. A complex comprising ThiI and a truncated tRNA was prepared and cry
Autor:
Charles T. Lauhon
Publikováno v:
Biochemistry. 51:8950-8963
Genetic and biochemical studies have recently implicated four proteins required in bacteria for the biosynthesis of the universal tRNA modified base N6-threonylcarbamoyl adenosine (t(6)A). In this work, t(6)A biosynthesis in Bacillus subtilis has bee
Autor:
Brett J. Kopina, Charles T. Lauhon
Publikováno v:
Organic Letters. 14:4118-4121
An efficient route for the synthesis of 2,4-diaminopyrimidine ribosides from cytidine is described consisting of six steps with overall yields >50% and only one chromatographic step. The key amine addition step utilizes LiCl and 1,8-diazabicyclo[5.4.
Publikováno v:
Journal of Biological Chemistry. 279:19551-19558
IscS catalyzes the fragmentation of l-cysteine to l-alanine and sulfane sulfur in the form of a cysteine persulfide in the active site of the enzyme. In Escherichia coli IscS, the active site cysteine Cys(328) resides in a flexible loop that potentia
Publikováno v:
Journal of Biological Chemistry. 279:23022-23029
The biosynthesis of 4-thiouridine (s4U) in Escherichia coli tRNA requires the action of both the thiamin pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from l-cysteine to ThiI, which utilizes Mg-ATP to activate
Autor:
Timothy J. Larson, Matt D. Wolfe, Farzana Ahmed, Thressa C. Stadtman, Charles T. Lauhon, Gerard M. Lacourciere
Publikováno v:
Journal of Biological Chemistry. 279:1801-1809
Escherichia coli has eight genes predicted to encode sulfurtransferases having the active site consensus sequence Cys-Xaa-Xaa-Gly. One of these genes, ybbB, is frequently found within bacterial operons that contain selD, the selenophosphate synthetas
Autor:
Ravi Kambampati, Charles T. Lauhon
Publikováno v:
Biochemistry. 42:1109-1117
Thionucleosides are uniquely present in tRNA. In many organisms, tRNA specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome b
Autor:
Charles T. Lauhon
Publikováno v:
Journal of Bacteriology. 184:6820-6829
Escherichia coli tRNA contains four naturally occurring nucleosides modified with sulfur. Cysteine is the intracellular sulfur source for each of these modified bases. We previously found that the iscS gene, a member of the nifS cysteine desulfurase