ArticleThe Journal of biological chemistry2010
Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Article
- Distinct pathogenic mechanisms of various RARS1 mutations in Pelizaeus-Merzbacher-like disease.Science China. Life sciences · 2021Article
- An Analysis of the Multifaceted Roles of Heme in the Pathogenesis of Cancer and Related Diseases.Cancers · 2021Review
- Quantification of Active Apohemoglobin Heme-Binding Sites via Dicyanohemin Incorporation.Biochemistry · 2017Article
- Delineating distinct heme-scavenging and -binding functions of domains in MF6p/helminth defense molecule (HDM) proteins from parasitic flatworms.The Journal of biological chemistry · 2017Article
- Quantification of labile heme in live malaria parasites using a genetically encoded biosensor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall inFrontiers in cellular and infection microbiology · 2016Article
- Inhibition of arginyltransferase 1 induces transcriptional activity of myocardin-related transcription factor A (MRTF-A) and promotes directional migration.The Journal of biological chemistry · 2014Article
- The mRNA of human cytoplasmic arginyl-tRNA synthetase recruits prokaryotic ribosomes independently.The Journal of biological chemistry · 2014Article
- Iron metabolism regulates p53 signaling through direct heme-p53 interaction and modulation of p53 localization, stability, and function.Cell reports · 2014Article
- Article
- Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase.Biochemistry · 2012Article
- Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis.Biochemical pharmacology · 2012Article
- The N-end rule pathway.Annual review of biochemistry · 2012Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The free form of human cytoplasmic arginyl-tRNA synthetase (hcArgRS) is hypothesized to participate in ubiquitin-dependent protein degradation by offering arginyl-tRNA(Arg) to arginyl-tRNA transferase (ATE1). We investigated the effect of hemin on hcArgRS based on the fact that hemin regulates several critical proteins in the "N-end rule" protein degradation pathway. Extensive biochemical evidence has established that hemin could bind to both forms of hcArgRS in vitro. Based on the spectral changes of the Soret band on site-directed protein mutants, we identified Cys-115 as a specific axial ligand of hemin binding that is located in the Add1 domain. Hemin inhibited the catalytic activity of full-length and N-terminal 72-amino acid-truncated hcArgRSs by blocking amino acid activation. Kinetic analysis demonstrated that the K(m) values for tRNA(Arg), arginine, and ATP in the presence of hemin were not altered, but k(cat) values dramatically decreased compared with those in the absence of hemin. By comparison, the activity of prokaryotic ArgRS was not affected obviously by hemin. Gel filtration chromatography suggested that hemin induced oligomerization of both the isolated Add1 domain and the wild type enzyme, which could account for the inhibition of catalytic activity. However, the catalytic activity of an hcArgRS mutant with Cys-115 replaced by alanine (hcArgRS-C115A) was also inhibited by hemin, suggesting that hemin binding to Cys-115 is not responsible for the inhibition of enzymatic activity and that the specific binding may participate in other biological functions.
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