Inhibition of proteolytic processing of the polyproteins of cowpea mosaic virus by hemin.
Cleavages of the polyproteins synthesized from cowpea mosaic virus (CPMV) B RNA and M RNA in rabbit reticulocyte lysates are inhibited by hemin. Cleavage of the CPMV B RNA-encoded 200K polyprotein and of the M RNA-encoded 60K intermediary precursor protein were most sensitive to hemin inhibition, while cleavages of other precursor proteins were less sensitive. A significant observation was that at a hemin concentration of 25 microM, but not at higher concentrations, the 60K protein was cleaved to yield the two viral capsid proteins. This cleavage reaction has not been observed in vitro previously.
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Department of Biochemistry, Louisiana State University, Baton Rouge.
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D004591:Electrophoresis, Polyacrylamide Gel; D006418:Heme / Q000031:analogs & derivatives*; D006427:Hemin / Q000494:pharmacology*; D009029:Mosaic Viruses / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000378:metabolism; D012367:RNA, Viral / Q000235:genetics; D014764:Viral Proteins / Q000096:biosynthesis / Q000378:metabolism*
D011498:Protein Precursors; D012367:RNA, Viral; D014764:Viral Proteins; D006418:Heme; D006427:Hemin