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Originally published In Press as doi:10.1074/jbc.M102576200 on April 6, 2001

J. Biol. Chem., Vol. 276, Issue 25, 22056-22063, June 22, 2001
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Sequence Properties of the 1,2-Diacylglycerol 3-Glucosyltransferase from Acholeplasma laidlawii Membranes
RECOGNITION OF A LARGE GROUP OF LIPID GLYCOSYLTRANSFERASES IN EUBACTERIA AND ARCHAEA*

Stefan BergDagger §, Maria EdmanDagger §, Lu LiDagger , Malin Wikström, and Åke Wieslander||

From the Dagger  Department of Biochemistry, Umeå University, S-901 87 Umeå, Sweden and the  Department of Biochemistry and Biophysics, Stockholm University, S-106 91 Stockholm, Sweden

Synthesis of the nonbilayer-prone alpha -monoglucosyldiacylglycerol (MGlcDAG) is crucial for bilayer packing properties and the lipid surface charge density in the membrane of Acholeplasma laidlawii. The gene for the responsible, membrane-bound glucosyltransferase (alMGS) (EC 2.4.1.157) was sequenced and functionally cloned in Escherichia coli, yielding MGlcDAG in the recombinants. Similar amino acid sequences were encoded in the genomes of several Gram-positive bacteria (especially pathogens), thermophiles, archaea, and a few eukaryotes. All of these contained the typical EX7E catalytic motif of the CAZy family 4 of alpha -glycosyltransferases. The synthesis of MGlcDAG by a close sequence analog from Streptococcus pneumoniae (spMGS) was verified by polymerase chain reaction cloning, corroborating a connection between sequence and functional similarity for these proteins. However, alMGS and spMGS varied in dependence on anionic phospholipid activators phosphatidylglycerol and cardiolipin, suggesting certain regulatory differences. Fold predictions strongly indicated a similarity for alMGS (and spMGS) with the two-domain structure of the E. coli MurG cell envelope glycosyltransferase and several amphipathic membrane-binding segments in various proteins. On the basis of this structure, the alMGS sequence charge distribution, and anionic phospholipid dependence, a model for the bilayer surface binding and activity is proposed for this regulatory enzyme.

* This work was supported by the Swedish Natural Science Research Council.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF349769.

§ These authors contributed equally to this work.

|| To whom correspondence should be addressed. Tel.: 46-8-16-24-63; Fax: 46-8-15-36-79; E-mail: ake@dbb.su.se.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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