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.