Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA.
The 5' end of porcine mitochondrial aconitase mRNA contains an iron responsive element (IRE)-like secondary structure (T. Dandekar, R. Stripecke, N. K. Gray, B. Goosen, A. Constable, H. E. Johansson, and M. W. Hentze (1991) EMBO J. 10, 1903-1909). A protein from a liver extract binds to a mitochondrial aconitase RNA probe and supports the identification of this sequence as an IRE. Purified cytosolic aconitase but not the mitochondrial enzyme binds to this IRE as well as to a ferritin IRE. All forms of cytosolic aconitase, [4Fe-4S] enzyme, [3Fe-4S] enzyme and apoenzyme bind with similar affinity. A Kd of 0.25 nM was calculated for the apoaconitase-IRE interaction from Scatchard analysis. These results support the conclusion that cytosolic aconitase is an IRE-binding protein which may regulate translation of mitochondrial aconitase mRNA.
Zheng
L
L
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-1153.
Kennedy
M C
MC
Blondin
G A
GA
Beinert
H
H
Zalkin
H
H
D000154:Aconitate Hydratase / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D002892:Chromosomes, Human, Pair 22; D002899:Chromosomes, Human, Pair 9; D003600:Cytosol / Q000201:enzymology; D005293:Ferritins / Q000235:genetics; D005786:Gene Expression Regulation; D006801:Humans; D007501:Iron / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism; D012045:Regulatory Sequences, Nucleic Acid; D012261:Ribonucleoproteins / Q000378:metabolism
D009838:Oligodeoxyribonucleotides; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D005293:Ferritins; D007501:Iron; D000154:Aconitate Hydratase