Lipid dependence and activity control of phosphatidylserine synthase from <i>Escherichia coli</i>

Linde, Kajsa; Gröbner, Gerhard; Rilfors, Leif

doi:10.1016/j.febslet.2004.08.038

Cited by 16 publications

(15 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4). Similar effects on the activity by PG and CL have also been observed for phosphatidylserine synthase from E. coli (Linde et al ., 2004). This is probably an important feature for interface enzymes having lipids as substrates, and will give the enzymes an ability to sense the properties of the membrane and to perform the proper reaction.…”

Section: Resultssupporting

confidence: 78%

A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: involvement in host immune response

Klement¹,

Öjemyr²,

Tagscherer

et al. 2007

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe human pathogen Mycoplasma pneumoniae has a very small genome but with many yet not identified gene functions, e.g. for membrane lipid biosynthesis. Extensive radioactive labelling in vivo and enzyme assays in vitro revealed a substantial capacity for membrane glycolipid biosynthesis, yielding three glycolipids, five phosphoglycolipids, in addition to six phospholipids. Most glycolipids were synthesized in a cell protein/lipid-detergent extract in vitro; galactose was incorporated into all species, whereas glucose only into a few. One (MPN483) of the three predicted glycosyltransferases (GTs; all essential) was both processive and promiscuous, synthesizing most of the identified glycolipids. These enzymes are of a GT-A fold, similar to an established structure, and belong to CAZy GT-family 2. The cloned MPN483 could use both diacylglycerol (DAG) and human ceramide acceptor substrates, and in particular UDPgalactose but also UDP-glucose as donors, making mono-, di-and trihexose variants. MPN483 output and processitivity was strongly influenced by the local lipid environment of anionic lipids. The structure of a major b1,6GlcbGalDAG species was determined by NMR spectroscopy. This, as well as other purified M. pneumoniae glycolipid species, is important antigens in early infections, as revealed from ELISA screens with patient IgM sera, highlighting new aspects of glycolipid function.

show abstract

Section: Resultssupporting

confidence: 78%

A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: involvement in host immune response

Klement¹,

Öjemyr²,

Tagscherer

et al. 2007

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…The increased level of the tetraacylated DPG and simultaneous decrease in the percentage of PG can contribute to elevation in the phase transition temperature of lipids from Y. pseudotuberculosis, which appears to enhance the tolerance of bacteria to stress and may reflect a requirement for enhancement of the structural integrity of the cell membrane [24]. Unlike PG, DPG has a tendency to form reversed hexagonal phases and is likely to increase packing density in the apolar as well as the polar parts of the bilayer [25,26]. Both these effects decrease the ability of proteins to penetrate the hydrophobic environment [27].…”

Section: Discussionmentioning

confidence: 99%

Effect of phenol‐induced changes in lipid composition on conformation of OmpF‐like porin of Yersinia pseudotuberculosis

et al. 2013

View full text Add to dashboard Cite

a b s t r a c tThe present work aimed to compare the effects of different lysophosphatidylethanolamine (LPE) content in lipids derived from Yersinia pseudotuberculosis cells exposed and not exposed to phenol on the conformation of OmpF-like porin of these bacteria. Differential scanning calorimetry and intrinsic protein fluorescence showed that the 2.5-fold increase of LPE content and the corresponding increase in the phase transition temperature of bacterial lipids were accompanied by enhanced protein thermostability. Integral conformational rearrangement of protein was supported by drastic changes in the microenvironment of the tryptophan residues, likely resulting in a convergence of monomers in trimeric porin and exposure of outer tryptophan residues to the water environment. These conformational changes may impede the porin channel permeability under stress conditions in bacteria.

show abstract

“…E. coli PS synthase was reconstituted into lipid vesicles of defined phospholipid compositions and the activity of the enzyme was found to be stimulated by the anionic lipids phosphatidylglycerol, cardiolipin and phosphatidic acid [63,64]. This mode of regulation of PS synthase might be physiologically relevant for maintaining the balance among the levels of phosphatidylglycerol and cardiolipin on one hand, and PE (which is derived from PS) on the other hand.…”

Section: Regulation Of Ps Synthesis In E Colimentioning

confidence: 96%

Metabolism and functions of phosphatidylserine

Vance

Steenbergen

2005

Progress in Lipid Research

441

402

View full text Add to dashboard Cite

Lipid dependence and activity control of phosphatidylserine synthase from Escherichia coli

Cited by 16 publications

References 26 publications

A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: involvement in host immune response

A processive lipid glycosyltransferase in the small human pathogen Mycoplasma pneumoniae: involvement in host immune response

Effect of phenol‐induced changes in lipid composition on conformation of OmpF‐like porin of Yersinia pseudotuberculosis

Metabolism and functions of phosphatidylserine

Contact Info

Product

Resources

About