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Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium occurs in two principally distinct pathways

Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium occurs in two principally distinct pathways. Leipuviene, Ramune; Qian, Qiang; Bjoerk, Glenn R. (Department of Molecular Biology, Umea University, Umea S-90187, Swed.). Journal of Bacteriology, 186(3), 758-766 (English) 2004 American Society for Microbiology. CODEN: JOBAAY. There are some commonly used reagents like 13239-97-9 in this article. ISSN: 0021-9193. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) Section cross-reference(s): 6 TRNA from Salmonella enterica serovar Typhimurium contains five thiolated nucleosides, 2-thiocytidine (s2C), 4-thiouridine (s4U), 5-methylaminomethyl-2-thiouridine (mnm5s2U), 5-carboxymethylaminomethyl-2-thiouridine (cmnm5s2U), and N-6-(4-hydroxyisopentenyl)-2-methylthioadenosine (ms2io6A). The levels of all of them are significantly reduced in cells with a mutated iscS gene, which encodes the cysteine desulfurase IscS, a member of the ISC machinery that is responsible for [Fe-S] cluster formation in proteins. A mutant (iscU52) was isolated that carried an amino acid substitution (S107T) in the IscU protein, which functions as a major scaffold in the formation of [Fe-S] clusters. In contrast to the iscS mutant, the iscU52 mutant showed reduced levels of only two of the thiolated nucleosides, ms2io6A (10-fold) and s2C (more than 2-fold). Deletions of the iscU, hscA, or fdx genes from the isc operon lead to a similar tRNA thiolation pattern to that seen for the iscU52 mutant.Several substances like 13239-97-9 may be metioned in this study. Unexpectedly, deletion of the iscA gene, coding for an alternative scaffold protein for the [Fe-S] clusters, showed a novel tRNA thiolation pattern, where the synthesis of only one thiolated nucleoside, ms2io6A, was decreased twofold. Based on our results, we suggest two principal distinct routes for thiolation of tRNA: (i) a direct sulfur transfer from IscS to the tRNA modifying enzymes ThiI and MnmA, which form s4U and the s2U moiety of (c)mnm5s2U, resp.; and (ii) an involvement of [Fe-S] proteins (an unidentified enzyme in the synthesis of s2C and MiaB in the synthesis of ms2io6A) in the transfer of sulfur to the tRNA. ..

Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium occurs in two principally distinct pathways

Formation of thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium occurs in two principally distinct pathways. Leipuviene, Ramune; Qian, Qiang; Bjoerk, Glenn R. (Department of Molecular Biology, Umea University, Umea S-90187, Swed.). Journal of Bacteriology, 186(3), 758-766 (English) 2004 American Society for Microbiology. CODEN: JOBAAY. There are some commonly used reagents like 13239-97-9 in this article. ISSN: 0021-9193. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) Section cross-reference(s): 6 TRNA from Salmonella enterica serovar Typhimurium contains five thiolated nucleosides, 2-thiocytidine (s2C), 4-thiouridine (s4U), 5-methylaminomethyl-2-thiouridine (mnm5s2U), 5-carboxymethylaminomethyl-2-thiouridine (cmnm5s2U), and N-6-(4-hydroxyisopentenyl)-2-methylthioadenosine (ms2io6A). The levels of all of them are significantly reduced in cells with a mutated iscS gene, which encodes the cysteine desulfurase IscS, a member of the ISC machinery that is responsible for [Fe-S] cluster formation in proteins. A mutant (iscU52) was isolated that carried an amino acid substitution (S107T) in the IscU protein, which functions as a major scaffold in the formation of [Fe-S] clusters. In contrast to the iscS mutant, the iscU52 mutant showed reduced levels of only two of the thiolated nucleosides, ms2io6A (10-fold) and s2C (more than 2-fold). Deletions of the iscU, hscA, or fdx genes from the isc operon lead to a similar tRNA thiolation pattern to that seen for the iscU52 mutant.Several substances like 13239-97-9 may be metioned in this study. Unexpectedly, deletion of the iscA gene, coding for an alternative scaffold protein for the [Fe-S] clusters, showed a novel tRNA thiolation pattern, where the synthesis of only one thiolated nucleoside, ms2io6A, was decreased twofold. Based on our results, we suggest two principal distinct routes for thiolation of tRNA: (i) a direct sulfur transfer from IscS to the tRNA modifying enzymes ThiI and MnmA, which form s4U and the s2U moiety of (c)mnm5s2U, resp.; and (ii) an involvement of [Fe-S] proteins (an unidentified enzyme in the synthesis of s2C and MiaB in the synthesis of ms2io6A) in the transfer of sulfur to the tRNA. ..