ArticleThe Journal of biological chemistry2010
The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Article
- Fe-S cluster assembly in the supergroup Excavata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Diverse Mechanisms of Sulfur Decoration in Bacterial tRNA and Their Cellular Functions.Biomolecules · 2017Review
- Understanding the role of dynamics in the iron sulfur cluster molecular machine.Biochimica et biophysica acta. General subjects · 2017Article
- A tRNA methyltransferase paralog is important for ribosome stability and cell division in Trypanosoma brucei.Scientific reports · 2016Article
- The Eukaryotic-Specific ISD11 Is a Complex-Orphan Protein with Ability to Bind the Prokaryotic IscS.PloS one · 2016Article
- A common tRNA modification at an unusual location: the discovery of wyosine biosynthesis in mitochondria.Nucleic acids research · 2015Article
- Article
- Mitochondrial and nucleolar localization of cysteine desulfurase Nfs and the scaffold protein Isu in Trypanosoma brucei.Eukaryotic cell · 2014Article
- The T. brucei TRM5 methyltransferase plays an essential role in mitochondrial protein synthesis and function.RNA (New York, N.Y.) · 2013Article
- The suf iron-sulfur cluster synthesis pathway is required for apicoplast maintenance in malaria parasites.PLoS pathogens · 2013Article
- Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Enigmatic presence of mitochondrial complex I in Trypanosoma brucei bloodstream forms.Eukaryotic cell · 2012Article
- Isd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein.The Journal of biological chemistry · 2011Article
- Assembling Fe/S-clusters and modifying tRNAs: ancient co-factors meet ancient adaptors.Trends in parasitology · 2011Article
- Transfer RNA modifications: nature's combinatorial chemistry playground.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Fe/S clusters are part of the active site of many enzymes and are essential for cell viability. In eukaryotes the cysteine desulfurase Nfs (IscS) donates the sulfur during Fe/S cluster assembly and was thought sufficient for this reaction. Moreover, Nfs is indispensable for tRNA thiolation, a modification generally required for tRNA function and protein synthesis. Recently, Isd11 was discovered as an integral part of the Nfs activity at an early step of Fe/S cluster assembly. Here we show, using a combination of genetic, molecular, and biochemical approaches, that Isd11, in line with its strong association with Nfs, is localized in the mitochondrion of T. brucei. In addition to its involvement in Fe/S assembly, Isd11 also partakes in both cytoplasmic and mitochondrial tRNA thiolation, whereas Mtu1, another protein proposed to collaborate with Nfs in tRNA thiolation, is required for this process solely within the mitochondrion. Taken together these data place Isd11 at the center of these sulfur transactions and raises the possibility of a connection between Fe/S metabolism and protein synthesis, helping integrate two seemingly unrelated pathways.
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