Pulse labelling experiments with [S-35]L-methionine were performed to
determine the rate of protein synthesis. Treatment of cultured cells o
f peanut with fungal cell wall led to a drastic increase in the de nov
o synthesis of particular proteins in the cytosol, the endoplasmic ret
iculum and the extracellular compartment. In the nucleus, a single new
ly synthesized protein, designated p 56, was detectable upon elicitati
on by fungal elicitor. Pulse labelling with [S-35]L-methionine for 1 h
was applied at various times following elicitation. The time course o
f p 56 biosynthesis was transient and the maximum of p 56 de novo synt
hesis preceded the one of the cytosolic protein stilbene synthase. The
preferential de novo synthesis and transfer of p 56 to the nucleus, o
nly briefly before the elicitor-triggered signal chain causes the acti
vation of nuclear defence genes, makes it a good candidate as member o
f the signal transduction machinery to the nucleus. p 56 was further c
haracterized by its size as N-octyl-beta-D-glucoside micelle. Selectiv
e solubilization experiments showed that p 56 is a hydrophobic, not sa
lt extractable protein rather well protected against partial proteolys
is.