Mitochondrial Aconitase Binds to the 3’-UTR of Mouse Hepatitis Virus RNA
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Cis-acting signals located in the 3’-UTR of the viral genome were first identified by deletion analyses of MHV defective interfering (DI)-RNAs (Kim, Jeong, and Makino, 1993; Lin and Lai, 1993). The cis-acting signals for the synthesis of minus-strand RNA are contained within the last 55 nucleotides (nt) plus the poly (A) tail (Lin, Liao, and Lai, 1994). Our lab has previously shown that host cell proteins specifically bind to two distinct sites within the MHV 3’UTR (Yu and Leibowitz, 1995b). In the current work, we show that the RNA-protein (RNP) complex formed within the last 42 nt of the genomic RNA contains four proteins of molecular mass 90, 70, 58 and 40 kDa and identify the 90 kDa protein as mitochondrial aconitase.
KeywordsFerric Ammonium Citrate Mouse Hepatitis Virus Iron Regulatory Protein Defective Interfere Mitochondrial Aconitase
- Yu, W., and Leibowitz, J. L. (1995b). Specific binding of host cellular proteins to multiple sites within the 3‱ end of mouse hepatitis virus genomic RNA. J. Virol. 69, 5033–5038.Google Scholar