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Dissection of membrane-binding and -remodeling regions in two classes of bacterial phospholipid N-methyltransferases.
- Source :
-
Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2017 Dec; Vol. 1859 (12), pp. 2279-2288. Date of Electronic Publication: 2017 Sep 11. - Publication Year :
- 2017
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Abstract
- Bacterial phospholipid N-methyltransferases (Pmts) catalyze the formation of phosphatidylcholine (PC) via successive N-methylation of phosphatidylethanolamine (PE). They are classified into Sinorhizobium-type and Rhodobacter-type enzymes. The Sinorhizobium-type PmtA protein from the plant pathogen Agrobacterium tumefaciens is recruited to anionic lipids in the cytoplasmic membrane via two amphipathic helices called αA and αF. Besides its enzymatic activity, PmtA is able to remodel membranes mediated by the αA domain. According to the Heliquest program, αA- and αF-like amphipathic helices are also present in other Sinorhizobium- and Rhodobacter-type Pmt enzymes suggesting a conserved architecture of α-helical membrane-binding regions in these methyltransferases. As representatives of the two Pmt families, we investigated the membrane binding and remodeling capacity of Bradyrhizobium japonicum PmtA (Sinorhizobium-type) and PmtX1 (Rhodobacter-type), which act cooperatively to produce PC in consecutive methylation steps. We found that the αA regions in both enzymes bind anionic lipids similar to αA of A. tumefaciens PmtA. Membrane binding of PmtX1 αA is enhanced by its substrate monomethyl-PE indicating a substrate-controlled membrane association. The αA regions of all investigated enzymes remodel spherical liposomes into tubular filaments suggesting a conserved membrane-remodeling capacity of bacterial Pmts. Based on these results we propose that the molecular details of membrane-binding and remodeling are conserved among bacterial Pmts.<br /> (Copyright © 2017 Elsevier B.V. All rights reserved.)
- Subjects :
- Agrobacterium tumefaciens genetics
Amino Acid Sequence
Bacterial Proteins classification
Bacterial Proteins genetics
Bacterial Proteins metabolism
Binding Sites
Cell Membrane chemistry
Cell Membrane metabolism
Cloning, Molecular
Conserved Sequence
Escherichia coli enzymology
Escherichia coli genetics
Gene Expression
Genetic Vectors chemistry
Genetic Vectors metabolism
Isoenzymes chemistry
Isoenzymes classification
Isoenzymes genetics
Isoenzymes metabolism
Liposomes metabolism
Methylation
Methyltransferases classification
Methyltransferases genetics
Methyltransferases metabolism
Phosphatidylcholines chemistry
Phosphatidylcholines metabolism
Phosphatidylethanolamines chemistry
Phosphatidylethanolamines metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Interaction Domains and Motifs
Recombinant Proteins chemistry
Recombinant Proteins classification
Recombinant Proteins genetics
Recombinant Proteins metabolism
Rhodobacter genetics
Sinorhizobium genetics
Substrate Specificity
Agrobacterium tumefaciens enzymology
Bacterial Proteins chemistry
Liposomes chemistry
Methyltransferases chemistry
Rhodobacter enzymology
Sinorhizobium enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0005-2736
- Volume :
- 1859
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta. Biomembranes
- Publication Type :
- Academic Journal
- Accession number :
- 28912104
- Full Text :
- https://doi.org/10.1016/j.bbamem.2017.09.013