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Use of limited proteolysis and mutagenesis to identify folding domains and sequence motifs critical for wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase activity

Abstract: Triacylglycerols and wax esters are synthesized as energy storage molecules by some proteobacteria and actinobacteria under stress. The enzyme responsible for neutral lipid accumulation is the bifunctional wax ester synthase/acyl-coenzyme A (CoA):diacylglycerol acyltransferase (WS/DGAT). Structural modeling of WS/DGAT suggests that it can adopt an acyl-CoA-dependent acyltransferase fold with the N-terminal and C-terminal domains connected by a helical linker, an architecture demonstrated experimentally by limited proteolysis. Moreover, we found that both domains form an active complex when coexpressed as independent polypeptides. The structural prediction and sequence alignment of different WS/DGAT proteins indicated catalytically important motifs in the enzyme. Their role was probed by measuring the activities of a series of alanine scanning mutants. Our study underscores the structural understanding of this protein family and paves the way for their modification to improve the production of neutral lipids.

Otras publicaciones de la misma revista o congreso con autores/as de la Universidad de Cantabria

 Fuente: Appl Environ Microbiol. 2014 Feb;80(3):1132-41

Editorial: American Society for Microbiology

 Año de publicación: 2014

Nº de páginas: 9

Tipo de publicación: Artículo de Revista

DOI: 10.1128/AEM.03433-13

ISSN: 0099-2240,1098-5336

Url de la publicación: http://dx.doi.org/10.1128/AEM.03433-13

Autores/as

VILLA TORRECILLA, JUAN ANTONIO

MATILDE ANDREA CABEZAS ISIDRO