scholarly journals Lyme Disease-Causing Borrelia Species Encode Multiple Lipoproteins Homologous to Peptide-Binding Proteins of ABC-Type Transporters

1998 ◽  
Vol 66 (9) ◽  
pp. 4115-4122 ◽  
Author(s):  
Jon A. Kornacki ◽  
Donald B. Oliver
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Lyme Disease ◽  
Dna Hybridization ◽  
Binding Proteins ◽  
Cell Envelope ◽  
Peptide Binding ◽  
Amino Acid Sequences ◽  
Linear Chromosome ◽  
Homologous Genes

ABSTRACT To identify cell envelope proteins of Borrelia burgdorferi, the causative agent of Lyme disease, we constructed a library of B. burgdorferi genes fused to the Escherichia coli phoA gene, which expresses enzymatically active alkaline phosphatase. One such gene, oppA-1, encodes a predicted polypeptide with significant similarities to various peptide-binding proteins of ABC-type transporters. Immediately downstream of oppA-1 are two genes, oppA-2 and oppA-3, whose predicted polypeptide products show strong similarities in their amino acid sequences to OppA-1, including a sequence that resembles the most highly conserved region in peptide-binding proteins. By labeling with [3H]palmitate, OppA-1, OppA-2, and OppA-3 were shown to be lipoproteins. DNA hybridization analysis showed that the oppA-1 oppA-2 oppA-3 region is located on the linear chromosome of B. burgdorferi, and the genes are conserved among different Borrelia species that cause Lyme disease (B. burgdorferi, B. garinii, and B. afzelli), suggesting that all three homologous genes are important to the maintenance of Lyme disease spirochetes in one or more of their hosts.

scholarly journals Complete Amino-Acid Sequences of DNA-Binding Proteins HU-1 and HU-2 from Escherichia coli

1980 ◽  
Vol 103 (3) ◽  
pp. 456-461
Author(s):  
B. Laine ◽  
D. Kmiecik ◽  
P. Sautiere ◽  
G. Biserte ◽  
M. Cohen-Solal
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Amino Acid Sequences

Complete Amino-Acid Sequences of DNA-Binding Proteins HU-1 and HU-2 from Escherichia coli

1980 ◽  
Vol 103 (3) ◽  
pp. 447-461 ◽  
Author(s):  
Bernard LAINE ◽  
Daniel KMIECIK ◽  
Pierre SAUTIERE ◽  
Gerard BISERTE ◽  
Michel COHEN-SOLAL
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Amino Acid Sequences

scholarly journals SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli

mBio ◽  
2020 ◽  
Vol 11 (6) ◽  
Author(s):  
Manuel Pazos ◽  
Katharina Peters ◽  
Adrien Boes ◽  
Yalda Safaei ◽  
Calem Kenward ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Binding Proteins ◽  
Cell Envelope ◽  
Synthetic Activity ◽  
Penicillin Binding Protein ◽  
Direct Role ◽  
Content Type ◽  
Class A

ABSTRACT Sporulation-related repeat (SPOR) domains are present in many bacterial cell envelope proteins and are known to bind peptidoglycan. Escherichia coli contains four SPOR proteins, DamX, DedD, FtsN, and RlpA, of which FtsN is essential for septal peptidoglycan synthesis. DamX and DedD may also play a role in cell division, based on mild cell division defects observed in strains lacking these SPOR domain proteins. Here, we show by nuclear magnetic resonance (NMR) spectroscopy that the periplasmic part of DedD consists of a disordered region followed by a canonical SPOR domain with a structure similar to that of the SPOR domains of FtsN, DamX, and RlpA. The absence of DamX or DedD decreases the functionality of the bifunctional transglycosylase-transpeptidase penicillin-binding protein 1B (PBP1B). DamX and DedD interact with PBP1B and stimulate its glycosyltransferase activity, and DamX also stimulates the transpeptidase activity. DedD also binds to PBP1A and stimulates its glycosyltransferase activity. Our data support a direct role of DamX and DedD in enhancing the activity of PBP1B and PBP1A, presumably during the synthesis of the cell division septum. IMPORTANCE Escherichia coli has four SPOR proteins that bind peptidoglycan, of which FtsN is essential for cell division. DamX and DedD are suggested to have semiredundant functions in cell division based on genetic evidence. Here, we solved the structure of the SPOR domain of DedD, and we show that both DamX and DedD interact with and stimulate the synthetic activity of the peptidoglycan synthases PBP1A and PBP1B, suggesting that these class A PBP enzymes act in concert with peptidoglycan-binding proteins during cell division.

The change in membrane phospholipid composition influences protein secretion and cell envelope biogenesis in Escherichia coli

2007 ◽  
Vol 2 (3) ◽  
pp. 385-404
Author(s):  
Alla Badyakina ◽  
Natalia Vasil’eva ◽  
Yulia Koryakina ◽  
Elena Anisimova ◽  
Natalia Suzina ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Protein Secretion ◽  
Culture Medium ◽  
Cytoplasmic Membrane ◽  
Cell Envelope ◽  
Phospholipid Composition ◽  
Barrier Properties ◽  
Phospholipid Metabolism ◽  
Membrane Phospholipids

AbstractSecretion of periplasmic alkaline phosphatase (PhoA) encoded by the gene constituent of plasmids and the peculiar properties of cell envelope biogenesis in Escherichia coli strains with controlled synthesis of individual membrane phospholipids have been studied. Alkaline phosphatase secretion across the cytoplasmic membrane declines, while secretion into the culture medium intensifies under changed metabolism. The composition of anionic membrane phospholipids changes due to inactivation of the pgsA gene or regulation of its expression by environmental factor, as well as in the absence of the pssA gene which is responsible for the synthesis of the precursor for zwitter-ionic phospholipid — phosphatidylethanolamine. This correlates with intensified secretion of exopolysaccharides and lower content of lipopolysaccharide and lipoprotein which are responsible for barrier properties of the outer membrane. The results suggest a possible coupling of protein secretion with biogenesis of cell envelope components at a level of phospholipid metabolism.

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