The effect of histone-mRNA interaction in protein synthesis.
The effect of lysine-rich and arginine-rich histones on selective inhibition of translation of mRNAs of tobacco mosaic virus (TMV), brome mosaic virus (BMV) and luciferase, in rabbit reticulocyte (RRL) was evaluated. Nuclease-treated RRL were supplemented with an appropriate mRNA and incubated with lysine-rich or arginine-rich histones at 5 and 2.5 micrograms/100 microliters lysate at 30 degrees C. Protein synthesis was measured as incorporation of 3H-leucine into protein for 24 min. The lysine-rich histone was more inhibitory than arginine-rich histone. At 5 and 2.5 micrograms/100 microliters lysate concentration, the lysine-rich histone inhibited translation of TMV mRNA by 57% and 35%, respectively, after 24 min. The corresponding values for arginine-rich histone were 31% and 13%. Both histones had a more inhibitory effect on the translation of viral mRNA than luciferase mRNA. Arginine-rich histone at 2.5 micrograms/100 microliters lysate did not cause any inhibition of luciferase mRNA. The spectrophotometric analysis of histone-mRNA mixtures at 280 nm indicated that, compared with arginine-rich histone, lysine-rich histone had a stronger affinity for mRNA.
Cheema
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Department of Biology, Bethune-Cookman College, Daytona Beach, Florida 32114, USA.
Hermann
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Scott
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Postell
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D000818:Animals; D001120:Arginine; D017795:Bromovirus / Q000235:genetics; D002474:Cell-Free System; D006657:Histones / Q000378:metabolism*; D008156:Luciferases / Q000235:genetics; D008239:Lysine; D014176:Protein Biosynthesis / Q000502:physiology*; D012333:RNA, Messenger / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism; D011817:Rabbits; D014027:Tobacco Mosaic Virus / Q000235:genetics; D014764:Viral Proteins / Q000096:biosynthesis
D006657:Histones; D012333:RNA, Messenger; D012367:RNA, Viral; D014764:Viral Proteins; D001120:Arginine; D008156:Luciferases; D008239:Lysine