Conserved Chromosomal Positions of Dual Domains of the ets Protooncogene in Cats, Mice, and Humans

The mammalian protooncogene homologue of the avian v-ets sequence from the E26 retrovirus consists of two sequentially distinct domains located on different chromosomes. Using somatic cell hybrid panels, we have mapped the mammalian homologue of the 5\u27 v-ets-domain to chromosome 11 (ETS1) in man, to chromosome 9 (Ets-1) in mouse, and to chromosome D1 (ETS1) in the domestic cat. The mammalian homologue of the 3\u27 v-ets domain was similarly mapped to human chromosome 21 (ETS2), to mouse chromosome 16 (Ets-2), and to feline chromosome C2 (ETS2). Both protooncogenes fell in syntenic groups of homologous linked loci that were conserved among the three species. The occurrence of two distinct functional protooncogenes and their conservation of linkage positions in the three mammalian orders indicate that these two genes have been separate since before the evolutionary divergence of mammals

Studies on Prolyl-tRNA Synthetase from E. Coli

Studies presented in this dissertation are concerned with both the isolation and characterization of prolyl-tRNA synthetase from E. coli. A detailed analysis of the amino acid binding site was undertaken as were kinetic studies leading to the establishment of the order of addition of substrates and release of products. Evidence that the enzyme possesses different areas for accepting the amino acid and tRNA has been presented; this was demonstrated by the differential affect of temperature on the activity of the enzyme as measured by ATP-PP exchange and esterification reactions. Some of the parameters involved in the interaction of synthetase with tRNA were examined by studying the effect of tRNA and modified tRNA on the protection of the enzyme against cold inactivation. Some of these results have been published previously (1,2,3)

The 3′-orf protein of human immunodeficiency virus shows structural homology with the phosphorylation domain of human interleukin-2 receptor and the ATP-binding site of the protein kinase family

AbstractThe primary amino acid sequence within a stretch of 25 residues (positions 91–116) of the middle portion of the 3-′orf protein (p273′-orf) of the human immunodeficiency virus (HIV) shares structural homology with a highly charged region within the intracytoplasmic phosphorylation domain of human interleukin-2 receptor (IL-2R) and the ATP-binding site of the catalytic subunit of cAMP-dependent protein kinase (cAMP-PK) and other members of the protein kinase family. Comparison of the predicted secondary structure within this region of p273′-orf with the phosphorylation domain of human IL-2R and the ATP-binding region of the phospho-kinase family of protein suggests that the 3′-orf protein could serve homologous function(s)