ArticleProceedings of the National Academy of Sciences of the United States of America2007
Regulation of a glutamyl-tRNA synthetase by the heme status.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 58 citations in OpenAlex.
- Systems metabolic engineering of dual pathways with stage-specific activation for high-level 5-aminolevulinic acid production inSynthetic and systems biotechnology · 2026Article
- A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria.Nature communications · 2024Article
- Natural 5-Aminolevulinic Acid: Sources, Biosynthesis, Detection and Applications.Frontiers in bioengineering and biotechnology · 2022Review
- Construction, analysis and validation of co-expression network to understand stress adaptation in Deinococcus radiodurans R1.PloS one · 2020Article
- 5-Aminolevulinic acid fermentation using engineered Saccharomyces cerevisiae.Microbial cell factories · 2019Article
- Dose-dependent effects of 1O2 in chloroplasts are determined by its timing and localization of production.Journal of experimental botany · 2019Review
- Physiological and transcriptomic analyses of a yellow-green mutant with high photosynthetic efficiency in wheat (Triticum aestivum L.).Functional & integrative genomics · 2018Article
- Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017Review
- Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology.Molecular microbiology · 2016Review
- Engineering Corynebacterium glutamicum to produce 5-aminolevulinic acid from glucose.Microbial cell factories · 2015Article
- Optimization of the heme biosynthesis pathway for the production of 5-aminolevulinic acid in Escherichia coli.Scientific reports · 2015Article
- Effect of hydrogen peroxide on the biosynthesis of heme and proteins: potential implications for the partitioning of Glu-tRNA(Glu) between these pathways.International journal of molecular sciences · 2014Article
- Gene expression profiling in Entamoeba histolytica identifies key components in iron uptake and metabolism.PloS one · 2014Article
- Thiol/Disulfide system plays a crucial role in redox protection in the acidophilic iron-oxidizing bacterium Leptospirillum ferriphilum.PloS one · 2012Article
- Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: the CAB domain plays a regulatory role, and region II is essential for catalysis.Plant physiology · 2011Article
- Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity.The Journal of biological chemistry · 2010Article
- Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation.Nucleic acids research · 2010Article
- Redox status affects the catalytic activity of glutamyl-tRNA synthetase.Biochemical and biophysical research communications · 2010Article
- tRNA as an active chemical scaffold for diverse chemical transformations.FEBS letters · 2010Review
- Selection and evaluation of reference genes for improved interrogation of microbial transcriptomes: case study with the extremophile Acidithiobacillus ferrooxidans.BMC molecular biology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamyl-tRNA (Glu-tRNA), formed by Glu-tRNA synthetase (GluRS), is a substrate for protein biosynthesis and tetrapyrrole formation by the C(5) pathway. In this route Glu-tRNA is transformed to delta-aminolevulinic acid, the universal precursor of tetrapyrroles (e.g., heme and chlorophyll) by the action of Glu-tRNA reductase (GluTR) and glutamate semialdehyde aminotransferase. GluTR is a target of feedback regulation by heme. In Acidithiobacillus ferrooxidans, an acidophilic bacterium that expresses two GluRSs (GluRS1 and GluRS2) with different tRNA specificity, the intracellular heme level varies depending on growth conditions. Under high heme requirement for respiration increased levels of GluRS and GluTR are observed. Strikingly, when intracellular heme is in excess, the cells respond by a dramatic decrease of GluRS activity and the level of GluTR. The recombinant GluRS1 enzyme is inhibited in vitro by hemin, but NADPH restores its activity. These results suggest that GluRS plays a major role in regulating the cellular level of heme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.