부산대학교 도서관

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.chembiol.2006.04.010 Byline: Kira J. Weissman (1), Hui Hong (1)(2), Bojana Popovic (1), Filip Meersman (2) Keywords: CHEMBIO Abstract: During biosynthesis on modular polyketide synthases (PKSs), chain extension intermediates are tethered to acyl carrier protein (ACP) domains through phosphopantetheinyl prosthetic groups. Each ACP must therefore interact with every other domain within the module, and also with a downstream acceptor domain. The nature of these interactions is key to our understanding of the topology and operation of these multienzymes. Sequence analysis and homology modeling implicates a potential helical region (helix II) on the ACPs as a protein-protein interaction motif. Using site-directed mutagenesis, we show that residues along this putative helix lie at the interface between the ACP and the phosphopantetheinyl transferase that catalyzes its activation. Our results accord with previous studies of discrete ACP proteins from fatty acid and aromatic polyketide biosynthesis, suggesting that helix II may also serve as a universal interaction motif in modular PKSs. Author Affiliation: (1) Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom (2) Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom Article History: Received 13 December 2005; Revised 24 April 2006; Accepted 25 April 2006 Article Note: (miscellaneous) Published: June 23, 2006