THE HUMAN AND BOVINE 14-3-3-ETA PROTEIN MESSENGER-RNAS ARE HIGHLY CONSERVED IN BOTH THEIR TRANSLATED AND UNTRANSLATED REGIONS

14-3-3 proteins form a highly conserved protein family whose members h ave been shown to activate tyrosine and tryptophan hydroxylases, inhib it protein kinase C and possess phospholipase A2 activity in vitro. We have isolated and analyzed a 14-3-3 protein cDNA clone (H14-3-3) from a human fetal brain cDNA library and found it to possess a high level of sequence identity with the bovine 14-3-3eta protein cDNA in both t he translated and untranslated regions, suggesting the presence of cis -regulatory elements in the untranslated regions of these mRNAs. The p roteins encoded by these two cDNAs are 98.4% identical. Two different sized RNA species, approx. 1.9 and 3.5 kb in size that are expressed i n a variety of tissues hybridize with this cDNA. However, only the 1.9 kb RNA is detected in the fetal brain. Northern blot analysis of poly (A)+ RNA isolated from eight different human tissues shows that 14-3-3 protein mRNAs are expressed in many tissues in the body. In agreement with previous reports, the highest abundance of RNA hybridizing with this cDNA is seen in the brain.