tailieunhanh - báo cáo khoa học: " Characterization of two Arabidopsis thaliana acyltransferases with preference for lysophosphatidylethanolamine"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Characterization of two Arabidopsis thaliana acyltransferases with preference for lysophosphatidylethanolamine | BMC Plant Biology BioMed Central Open Access Research article Characterization of two Arabidopsis thaliana acyltransferases with preference for lysophosphatidylethanolamine Kjell Stâlberg 1 Ulf Stâhl2 Sten Stymne2 and John Ohlrogge3 Address Department of Plant Biology and Forest Genetics Swedish University of Agricultural Sciences Box 7080 SE-750 07 Uppsala Sweden 2Department of Plant Breeding and Biotechnology Swedish University of Agricultural Sciences Box101 SE-230 53 Alnarp Sweden and 3Department of Plant Biology Michigan State University East Lansing MI 48824 USA Email Kjell Stâlberg - Ulf Stâhl - Sten Stymne - John Ohlrogge - ohlrogge@ Corresponding author Published 16 May 2009 Received 24 October 2008 BMC Plant Biology 2009 9 60 doi l47l-2229-9-60 Accepted 16 May 2009 This article is available from http l47l-2229 9 60 2009 Stẳlberg et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Two previously uncharacterized Arabidopsis genes that encode proteins with acyltransferase PlsC regions were selected for study based on their sequence similarity to a recently identified lung lysophosphatidylcholine acyltransferase LPCAT . To identify their substrate specificity and biochemical properties the two Arabidopsis acyltransferases designated AtLPEATl Atlg80950 and AtLPEAT2 At2g45670 were expressed in yeast knockout lines alel and slcl that are deficient in microsomal lysophosphatidyl acyltransferase activities. Results Expression of AtLPEATl in the yeast knockout alel background exhibited strong acylation activity of lysophosphatidylethanolamine LPE and lysophosphatidate LPA with lower activity on

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