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Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: the phosphoethanolamine transferase is encoded by opgE.

Bontemps-Gallo S, Cogez V, Robbe-Masselot C, Quintard K, Dondeyne J, Madec E, Lacroix JM - Biomed Res Int (2013)

Bottom Line: Osmoregulated periplasmic glucans (OPGs) are oligosaccharides found in the periplasm of many Gram-negative bacteria.In E. coli, OPG are substituted by phosphoglycerol and phosphoethanolamine derived from membrane phospholipids and by succinyl residues.Both genes show structural and functional similarities without sequence similarity.

View Article: PubMed Central - PubMed

Affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS 8576, IFR 147, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France ; Université Lille Nord de France, Lille, France.

ABSTRACT
Osmoregulated periplasmic glucans (OPGs) are oligosaccharides found in the periplasm of many Gram-negative bacteria. Glucose is the sole constitutive sugar and this backbone may be substituted by various kinds of molecules depending on the species. In E. coli, OPG are substituted by phosphoglycerol and phosphoethanolamine derived from membrane phospholipids and by succinyl residues. In this study, we describe the isolation of the opgE gene encoding the phosphoethanolamine transferase by a screen previously used for the isolation of the opgB gene encoding the phosphoglycerol transferase. Both genes show structural and functional similarities without sequence similarity.

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(a) Genetic organization of the opgE region. Chromosomal position of the opgE gene and Tn5 insertion of the opgE mutant isolated after the arbutin screen are indicated. (b) Predictive organization of the OpgE protein. Transmembrane segments are in grey, cytoplasmic regions are in blue, and periplasmic regions are in red and sulfatase domain within the last periplasmic region is shown. (c) Predictive model of the OpgE protein. First and last amino acids of the OpgE protein are indicated and first and last amino acids of each transmembrane (TM) segment are indicated.
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fig4: (a) Genetic organization of the opgE region. Chromosomal position of the opgE gene and Tn5 insertion of the opgE mutant isolated after the arbutin screen are indicated. (b) Predictive organization of the OpgE protein. Transmembrane segments are in grey, cytoplasmic regions are in blue, and periplasmic regions are in red and sulfatase domain within the last periplasmic region is shown. (c) Predictive model of the OpgE protein. First and last amino acids of the OpgE protein are indicated and first and last amino acids of each transmembrane (TM) segment are indicated.

Mentions: opgE is an operon constituted of one gene transcribed counterclockwise. The 1584 bp open reading frame begins at 851 820 bp and ends at 850 237 bp on the E. coli K12 chromosome and encodes a 527 amino acid protein (Figure 4) of 59 707 Da. The TMHMM2.0 algorithm [18] allowed the prediction of four transmembrane spanning segments in the 166 first amino acids and a periplasmic domain in the 361 following amino acids. The 217 to 483 amino acid sequence form a 226 amino acids catalytic domain with sulfuric ester hydrolase and transferase activities. Arbutin cannot cross the inner membrane of E. coli K12 strongly suggesting a periplasmic location of this catalytic domain. The OpgB protein shows a very similar organization [12] with 3 or 4 transmembrane segments in the 162 first amino acids followed by a periplasmic domain containing a 285 amino acids sulfuric ester hydrolase and transferase activities (amino acids 163 to 448) [12]. Despite the similarity between structure and function (except the donor phospholipid) of these two enzymes, no significant similarity was observed between the OpgB and OpgE amino acids sequences even in the hydrolase and transferase catalytic domains.


Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: the phosphoethanolamine transferase is encoded by opgE.

Bontemps-Gallo S, Cogez V, Robbe-Masselot C, Quintard K, Dondeyne J, Madec E, Lacroix JM - Biomed Res Int (2013)

(a) Genetic organization of the opgE region. Chromosomal position of the opgE gene and Tn5 insertion of the opgE mutant isolated after the arbutin screen are indicated. (b) Predictive organization of the OpgE protein. Transmembrane segments are in grey, cytoplasmic regions are in blue, and periplasmic regions are in red and sulfatase domain within the last periplasmic region is shown. (c) Predictive model of the OpgE protein. First and last amino acids of the OpgE protein are indicated and first and last amino acids of each transmembrane (TM) segment are indicated.
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Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC3818809&req=5

fig4: (a) Genetic organization of the opgE region. Chromosomal position of the opgE gene and Tn5 insertion of the opgE mutant isolated after the arbutin screen are indicated. (b) Predictive organization of the OpgE protein. Transmembrane segments are in grey, cytoplasmic regions are in blue, and periplasmic regions are in red and sulfatase domain within the last periplasmic region is shown. (c) Predictive model of the OpgE protein. First and last amino acids of the OpgE protein are indicated and first and last amino acids of each transmembrane (TM) segment are indicated.
Mentions: opgE is an operon constituted of one gene transcribed counterclockwise. The 1584 bp open reading frame begins at 851 820 bp and ends at 850 237 bp on the E. coli K12 chromosome and encodes a 527 amino acid protein (Figure 4) of 59 707 Da. The TMHMM2.0 algorithm [18] allowed the prediction of four transmembrane spanning segments in the 166 first amino acids and a periplasmic domain in the 361 following amino acids. The 217 to 483 amino acid sequence form a 226 amino acids catalytic domain with sulfuric ester hydrolase and transferase activities. Arbutin cannot cross the inner membrane of E. coli K12 strongly suggesting a periplasmic location of this catalytic domain. The OpgB protein shows a very similar organization [12] with 3 or 4 transmembrane segments in the 162 first amino acids followed by a periplasmic domain containing a 285 amino acids sulfuric ester hydrolase and transferase activities (amino acids 163 to 448) [12]. Despite the similarity between structure and function (except the donor phospholipid) of these two enzymes, no significant similarity was observed between the OpgB and OpgE amino acids sequences even in the hydrolase and transferase catalytic domains.

Bottom Line: Osmoregulated periplasmic glucans (OPGs) are oligosaccharides found in the periplasm of many Gram-negative bacteria.In E. coli, OPG are substituted by phosphoglycerol and phosphoethanolamine derived from membrane phospholipids and by succinyl residues.Both genes show structural and functional similarities without sequence similarity.

View Article: PubMed Central - PubMed

Affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS 8576, IFR 147, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France ; Université Lille Nord de France, Lille, France.

ABSTRACT
Osmoregulated periplasmic glucans (OPGs) are oligosaccharides found in the periplasm of many Gram-negative bacteria. Glucose is the sole constitutive sugar and this backbone may be substituted by various kinds of molecules depending on the species. In E. coli, OPG are substituted by phosphoglycerol and phosphoethanolamine derived from membrane phospholipids and by succinyl residues. In this study, we describe the isolation of the opgE gene encoding the phosphoethanolamine transferase by a screen previously used for the isolation of the opgB gene encoding the phosphoglycerol transferase. Both genes show structural and functional similarities without sequence similarity.

Show MeSH