TAILIEUCHUNG - Báo cáo khoa học: The isopenicillin N acyltransferases of Aspergillus nidulans and Penicillium chrysogenum differ in their ability to maintain the 40-kDa ab heterodimer in an undissociated form

The isopenicillin N acyltransferases (IATs) ofAspergillus nidulansandPenicilliumchrysogenumdiffered in their ability to maintain the 40-kDa proacyltransferaseabheterodimer in an undissociated form. The native A. nidulansIAT exhibited a molecular mass of 40 kDa by gel filtration. The P. chrysogenumIATshowedamolecularmassof 29 kDaby gel filtration (corresponding to the b subunit of the enzyme) but the undissociated 40-kDa heterodimer was never observed even in crude extracts. | Eur. J. Biochem. 270 1958-1968 2003 FEBS 2003 doi The isopenicillin N acyltransferases of Aspergillus nidulans and Penicillium chrysogenum differ in their ability to maintain the 40-kDa ab heterodimer in an undissociated form Francisco J. Fernandez1 Rosa E. Cardoza2 Eduardo Montenegro1 Javier Velasco1 Santiago Gutierrez1 2 and Juan F. Martin1 2 1Area de Microbiologia Facultad de Ciencias Biologicas y Ambientales Universidad de Leon Spain 2Instituto de Biotecnologia de Leon INBIOTEC Parque Cientlfico de León Spain The isopenicillin N acyltransferases IATs of Aspergillus nidulans and Penicillium chrysogenum differed in their ability to maintain the 40-kDa proacyltransferase ab heterodimer in an undissociated form. The native A. nidulans IAT exhibited a molecular mass of 40 kDa by gel filtration. The P. chrysogenum IAT showed a molecular mass of 29 kDaby gel filtration corresponding to the b subunit of the enzyme but the undissociated 40-kDa heterodimer was never observed even in crude extracts. Heterologous expression experiments showed that the chromatographic behaviour of IAT was determined by the source of the penDE gene used in the expression experiments and not by the host itself. When the penDE gene of A. nidulans was expressed in P. chrysogenum npe6 and npe8 or in Acremo-nium chrysogenum the IAT formed had a molecular mass of 40 kDa. On the other hand when the penDE gene originating from P. chrysogenum was expressed in A. chryso-genum the active IAT had a molecular mass of 29 kDa. The intronless form of the penDE gene cloned from an A. nidu-lans cDNA library and overexpressed in Escherichia coli formed the enzymatically active 40-kDa proIAT which was not self-processed as shown by immunoblotting with antibodies to IAT. This 40-kDa protein remained unprocessed even when treated with A. nidulans crude extract. In contrast the P. chrysogenum penDE intronless gene cloned from a cDNA library was expressed in E. coli and the IAT was

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