<> "The repository administrator has not yet configured an RDF license."^^ . <> . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants"^^ . "Protein N-terminal acetylation (Nt-acetylation) is the transfer of acetyl group from acetyl\r\ncoenzyme A (Ac-CoA) to the alpha amino acid of a protein. Since it has been discovered\r\nmore than fifty years ago, Nt-acetylation is known to be one of the most common protein\r\nmodifications in eukaryotes, occurring on approximately 50-70% of yeast soluble protein\r\nand about 80-90% of human protein. However, the exact biological role has remained\r\nenigmatic for majority of affected proteins, and only for a small number of proteins, Ntacetyation\r\nwas linked to various features of protein such as localization, stability and\r\ninteraction. Nt-acetylation in yeast and in human is thoroughly investigated with the\r\nidentification of five (NatA-NatE) and six (NatA-NatF) Nα-acetyltransferase (NAT) types,\r\nrespectively. In contrast, the knowledge of Nt-acetylation in plants was vacant for many\r\nyears. The first Arabidopsis NAT, AtNatC was identified in 2003, and very recently three\r\nmore NATs (NatA, NatB and NatE) were described by Iwona Stephan. In this study, we\r\nidentified two NATs (NatD and NatF) that are still missing in plants. AtNatD/AtNaa40p is\r\nconserved from yeast with respect to acetylation of protein histone H4. The lack of Nterminal\r\nserine acetylation increases the overall positive charge of H4 N-tail which causes\r\nthe minor phenotypes observed in atnaa40 mutant. The acetylation of N-terminal serine of\r\nhistone H4 might also involve in DNA double-strand break response. Besides, the\r\nsubcellular localization to cytoplasm and nucleus suggests a lysine acetyltransferase\r\nactivity of AtNaa40p towards histones. AtNatF/AtNaa60 unusually localizes to plasma\r\nmembrane and to the tonoplast. The sensitivity of atnaa60 mutant to salt tress during\r\ngermination stage appears to be related to the localization, and indicating the involvement\r\nof AtNaa60p in salt stress or osmotic stress response. Like hNaa60p, AtNaa60 is believed\r\nto acetylate a large number of proteins according to the NBD-Cl fluorescent assay.\r\nAtNaa60p acetylates methione and serine starting peptides in vitro.\r\nIn addition, numerous proteins are found N-terminally acetylated in chloroplasts, both\r\nchloroplast-encoded and nuclear-encoded proteins. In silico study reveals eight putative\r\nplastidic NATs of which seven localize to the chloroplasts when they are transiently\r\nexpressed with EYFP in Arabidopsis protoplasts. Three proteins (At2g39000, At1g24040\r\nand At2g06025) acetylate plenty of Escherichia coli proteins, their substrate specificities\r\nare strongly correlated to chlotoplast transit peptide (cTP) cleavage sites. Four other\r\nproteins (At4g19984, At1g26220, At1g32070 and At4g28030) are possibly true NATs\r\nsince they possess the conserved Ac-CoA binding motif. Our results, together with other\r\nstudies on acetylation in chloroplast, propose the connection between Nt-acetylation of\r\nchloroplastic proteins and drought stress."^^ . "2013" . . . . . . . . . . "Dinh-Van"^^ . "Trinh"^^ . "Dinh-Van Trinh"^^ . . "Trinh"^^ . "Dinh-Van"^^ . "Trinh Dinh-Van"^^ . . . . . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants (PDF)"^^ . . . "Trinh - Dissertation.pdf"^^ . . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants (Other)"^^ . . . . . . "indexcodes.txt"^^ . . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants (Other)"^^ . . . . . . "lightbox.jpg"^^ . . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants (Other)"^^ . . . . . . "preview.jpg"^^ . . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants (Other)"^^ . . . . . . "medium.jpg"^^ . . . "Missing links of the protein Nα-terminal\r\nacetylation machinery in plants (Other)"^^ . . . . . . "small.jpg"^^ . . "HTML Summary of #16019 \n\nMissing links of the protein Nα-terminal \nacetylation machinery in plants\n\n" . "text/html" . . . "570 Biowissenschaften, Biologie"@de . "570 Life sciences"@en . .