Dimerization of arginyl-tRNA synthetase by free heme drives its inactivation in plasmodium falciparum
Excess cellular heme is toxic, and malaria parasites regulate its levels during hemoglobin digestion. Aminoacyl-tRNA synthetases are ubiquitous enzymes, and of these, arginyl-tRNA synthetase (RRS) is unique as its enzymatic product of charged tRNA is required for protein synthesis and degradation. W...
Hauptverfasser: | Jain, V, Yogavel, M, Sharma, A |
---|---|
Format: | Journal article |
Veröffentlicht: |
Cell Press
2016
|
Ähnliche Einträge
Ähnliche Einträge
-
Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNA synthetase
von: Stanley C. Xie, et al.
Veröffentlicht: (2024-01-01) -
Drug targeting of one or more aminoacyl-tRNA synthetase in the malaria parasite Plasmodium falciparum
von: Manickam, Y, et al.
Veröffentlicht: (2018) -
The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.
von: Ariel McShane, et al.
Veröffentlicht: (2016-01-01) -
A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite <it>Plasmodium falciparum</it>
von: Santoni Daniele, et al.
Veröffentlicht: (2009-12-01) -
The structural basis of tRNA recognition by arginyl-tRNA-protein transferase
von: Thilini Abeywansha, et al.
Veröffentlicht: (2023-04-01)