TAILIEUCHUNG - Báo cáo khoa học: A 49 kDa microtubule cross-linking protein from Artemia franciscana is a coenzyme A-transferase

Embryos and larvae of the brine shrimp,Artemia francis-cana, were shown previously to possess a protein, now termed p49, which cross-links microtubules in vitro. Molecular characteristics of p49 were described, but the protein’s identity and its role in the cell were not determined. Degenerate oligonucleotide primers designed on the basis of peptide sequence obtained by Edman degradation during this studywereusedtogeneratep49cDNAsbyRT-PCRand thesewere clonedand sequenced. | Eur. J. Biochem. 270 4962-4972 2003 FEBS 2003 doi A 49 kDa microtubule cross-linking protein from Artemia franciscana is a coenzyme A-transferase Mindy M. Oulton1 Reinout Amons2 Ping Liang3 and Thomas H. MacRae1 1 Department of Biology Dalhousie University Halifax NS Canada department of Molecular Cell Biology Sylvius Laboratory Leiden the Netherlands 3Department of Cancer Genetics Roswell Park Cancer Institute Buffalo NY USA Embryos and larvae of the brine shrimp Artemia francis-cana were shown previously to possess a protein now termed p49 which cross-links microtubules in vitro. Molecular characteristics of p49 were described but the protein s identity and its role in the cell were not determined. Degenerate oligonucleotide primers designed on the basis of peptide sequence obtained by Edman degradation during this study were used to generate p49 cDNAs by RT-PCR and these were cloned and sequenced. Comparison with archived sequences revealed that the deduced amino acid sequence of p49 resembled the Drosophila gene product CG7920 as well as related proteins encoded in the genomes of Anopheles and Caenorhabditis. Similar proteins exist in several bacteria but no evident homologues were found in vertebrates and plants and only very distant homologues resided in yeast. When evolutionary relationships were compared p49 and the homologues from Drosophila Anopheles and Caenorhabditis formed a distinct subcluster within phylogenetic trees. Additionally the predicted secondary structures of p49 4-hydroxybutyrate CoA-transferase from Clostridium ami-nobutyricum and glutaconate CoA-transferase from Acid-aminococcus fermentans were similar and the enzymes may possess related catalytic mechanisms. The purified Artemia protein exhibited 4-hydroxybutyrate CoA-transferase activity thereby establishing p49 as the first crustacean CoA-transferase to be characterized. Probing of Western blots with an antibody against p49 revealed a cross-reactive .

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