Can I read Characterization of a non-reducing polyketide synthase gene from lichen Dirinaria applanata on EtoBox?

Characterization of a non-reducing polyketide synthase gene from lichen Dirinaria applanata by R. Valarmathi; G.N. Hariharan; Gayatri Venkataraman; Ajay Parida is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Characterization of a non-reducing polyketide synthase gene from lichen Dirinaria applanata about?

Lichens are known to produce a variety of secondary metabolites including polyketides that have diverse biological role(s). The biosynthesis of fungal polyketides is governed by type I polyketide synthases (PKS), enzymes with a multidomain structure, including the b-ketoacyl synthase (KS), acyl transferase (AT), ketoreductase (KR), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP) domains. Established soredial cultures of Dirinaria applanata (Fée) producing atranorin and divaricatic acid were used to characterize a polyketide synthase gene (DnPKS). A 743 bp fragment corresponding to the ketosynthase domain (KS) was isolated using degenerate primers. Complete sequence information for DnPKS (8162 bp) was obtained by walking in the 5 0 and 3 0 directions of the isolated KS domain using TAIL PCR. A translation of the DnPKS sequence identified the presence of KS, AT, two ACP and TE domains with eight intervening introns. TBLASTX analysis and comparison with other PKS sequences suggest that the coding region of DnPKS sequence is complete with the identification of putative start and stop codons and a stretch of 1226 upstream of the start codon corresponding to the put

Who reads Characterization of a non-reducing polyketide synthase gene from lichen Dirinaria applanata?

Author

R. Valarmathi; G.N. Hariharan; Gayatri Venkataraman; Ajay Parida

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0031-9422)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)