Nomura, K. H., Mizuguchi, S., Dejima, K., Murata, D., Matsuishi-Nakajima Y., Kawasaki, N., Gengyo-Ando, K., Mitani, S.4, Hirabayashi, Y., Nomura, K.. In eukaryotes, acetylation is the most common covalent modification out of over two hundred types of modifications reported to date. Among various acetylation, acetylation of??-amino group of lysine residues have been extensively studied in regard to "histone code" of epigenetic information transfer mechanism. Recently, lysine acetylation has been detected not only in nuclear histone/non-histone proteins but also in various proteins found in cytoplasm. One of the authors (Y. Hirabayashi) previously reported a cDNA cloning of mammalian acetyl-CoA transporter gene (AT-1; SLC33). The gene product is involved in O-acetylation of glycoconjugates in mammalian cells and its DNA sequence is well preserved from bacteria to human.. There is only one SLC33 orthologue (T26C5.3) in the nematode. We isolated intron deletion mutant (
tm246) and exon deletion mutant (
tm1317) of this gene by screening TMP/UV deletion mutant library. The mutant worm (
tm1317) showed decreased brood size (1/3 of N2), poor gonadal development but mantained in our laboratory for over 300 generations. In transgenically rescued
tm1317 mutant worm strains, T26C5.3::GFP fusion proteins are expressed in the head region, seam cells, spermatheca, vulva and the tail region. In this paper, we extracted proteins from wild type and these mutant worms, and analyzed proteomes of these animals with two dimensional (2D) electrophoresis. We differentiated more than 2,000 spots, and the spot patterns were analyzed with image analysis software. Two dimensional differential in-gel electrophoresis (2D-DIGE) technique was also used to compare proteomes between wild type and the mutant worms. About 500 spots showed over 1.5-fold increase in deletion mutant, and about 300 spots showed over 1.5-fold decrease in the mutant. Over 100 spots were picked up from the gel, and sequenced with LC/MS/MS to identify gene networks involved in development of mutant phenotypes. In this paper, we describe the results of transgenic expression analysis of the gene and report the results of proteome analysis (2D PAGE and 2D-DIGE). Among the proteins identified are paramyosin, intermediate filament proteins and ?-tubulin.