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A Drosophila gene structurally and functionally homologous to the mammalian 70-kDa S6 kinase gene

Watson, K.L., Chou, M.M., Blenis, J., Gelbart, W.M., Erikson, R.L.
Proceedings of the National Academy of Sciences of the United States of America 1996 v.93 no.24 pp. 13694-13698
messenger RNA, structural genes, complementary DNA, developmental stages, amino acid sequences, gene expression, ribosomes, chromosome mapping, ribosomal proteins, nucleotide sequences, phosphorylation, enzyme activity, polytene chromosomes, Drosophila melanogaster, hemocytes
cDNAs encoding the Drosophila 70-kDa S6 kinase (S6K) were isolated by low-stringency hybridization with mammalian p70S6k probes. Conceptual translation of S6k cDNA sequences yields a product containing all of the canonical features typical of serine/threonine kineses and has 78% amino acid identity in the catalytic domain with the human p70S6k homologue. The S6k gene, located at polytene chromosome site 65D, gives rise to two predominant transcripts of 3.0 and 5.0 kb and at least two smaller transcripts (<3.0 kb) that are found in whole-animal RNAs at all stages of development. Blood cells derived from the hematopoietic organs of ribosomal protein S6 (RpS6air8) mutant animals express higher levels of the smaller S6k transcripts, suggesting tissue- or genotype-specific differences in the regulation of the S6k gene. Drosophila S6K expressed in COS or NIH 3T3 cells phosphorylates mammalian RPS6 in a mitogen-dependent wortmannin- and rapamycin-sensitive manner, suggesting that its regulation is similiar to mammalian p70S6k.