Inhibition of poly(A)-binding protein synthesis in Friend erythroleukemia cells subsequent to heat shock.
When Friend erythroleukemia cells (FEC) are incubated at 43 degrees C there is a rapid and nearly complete inhibition of protein synthesis which can be reversed when cells are returned to their normal growing temperature of 37 degrees C. Examination of the recovery of FEC from heat shock indicates that most cellular mRNAs behave as a cohort and return to translation at approximately the same rate. We found a notable exception to this rule in the case of a 78 kDa basic protein (named protein A) whose rate of return to a normal synthetic rate is markedly inhibited subsequent to heat shock. We show that protein A corresponds to the 78 kDa polypeptide commonly found to be associated with the poly(A) tails of mammalian mRNA.
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D003593:Cytoplasm / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005622:Friend murine leukemia virus; D006358:Hot Temperature; D004915:Leukemia, Erythroblastic, Acute / Q000378:metabolism*; D008715:Methionine / Q000378:metabolism; D008970:Molecular Weight; D039102:Poly(A)-Binding Proteins; D012261:Ribonucleoproteins / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000096:biosynthesis; D013997:Time Factors
D002352:Carrier Proteins; D039102:Poly(A)-Binding Proteins; D012261:Ribonucleoproteins; D013205:Staphylococcal Protein A; C026452:messenger ribonucleoprotein; D008715:Methionine