TAILIEUCHUNG - Báo cáo khoa học: Molecular characterization of artemin and ferritin from Artemia franciscana

Embryos of the brine shrimp,Artemia franciscana, exhibit remarkable resistance to physiological stress, which is tem-porally correlated with the presence of two proteins, one a small heat shock/a-crystallin protein termed p26 and the other called artemin, of unknown was sequenced previously by Edman degradation, and its rela-tionship to ferritin, an iron storage protein, isolation from anArtemiaexpressed sequence tag library of artemin and ferritin cDNAs extends this work. . | Eur. J. Biochem. 270 137-145 2003 FEBS 2003 doi Molecular characterization of artemin and ferritin from Artemia franciscana Tao Chen1 I Reinout Amons2 James S. Clegg3 Alden H. Warner4 and Thomas H. MacRae1 1Department of Biology Dalhousie University Halifax Nova Scotia Canada department of Molecular Cell Biology Sylvius Laboratory Leiden the Netherlands dection of Molecular and Cellular Biology University of California Davis Bodega Bay CA USA department of Biological Sciences University of Windsor Windsor Ontario Canada Embryos of the brine shrimp Artemia franciscana exhibit remarkable resistance to physiological stress which is temporally correlated with the presence of two proteins one a small heat shock a-crystallin protein termed p26 and the other called artemin of unknown function. Artem in was sequenced previously by Edman degradation and its relationship to ferritin an iron storage protein established. The isolation from an Artemia expressed sequence tag library of artemin and ferritin cDNAs extends this work. Artemin cDNA was found to contain an ORF of 693 nucleotides and its deduced amino-acid sequence except for the initiator methionine was identical with that determined previously. Ferritin cDNA is 725 bp in length with an ORF of 516 nucleotides. Artemin ammo-acid residuss 3 1 5 are motl similar to ferritin but artemin is enriched in cysteines. Tie abundance of cysteines and their intramolecular spatial distribution suggest that artemin protects embryos against oxidative damage and or that its function is redox regulated. The conserved regions in artemin and ferritin monomers are structurally similar to one another and both proteins assemble into oligomers. However modeiíng ol the cpaierr-nary structure indicated that artemin multimers lack the central space used for metal storage that characterizes ferritin oligomers implying different roles for this protein. Probing of Northern blots revealed two artemin transcripts one

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