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The LysE Superfamily of Transport Proteins Involved in Cell Physiology and Pathogenesis.

Tsu BV, Saier MH - PLoS ONE (2015)

Bottom Line: Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication.Their common origin implies that they share common structural, mechanistic and functional attributes.The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Biology, Division of Biological Sciences, University of California at San Diego, La Jolla, California, United States of America.

ABSTRACT
The LysE superfamily consists of transmembrane transport proteins that catalyze export of amino acids, lipids and heavy metal ions. Statistical means were used to show that it includes newly identified families including transporters specific for (1) tellurium, (2) iron/lead, (3) manganese, (4) calcium, (5) nickel/cobalt, (6) amino acids, and (7) peptidoglycolipids as well as (8) one family of transmembrane electron carriers. Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication. Their common origin implies that they share common structural, mechanistic and functional attributes. The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations. They thus influence the physiology and pathogenesis of numerous microbes, being potential targets of drug action.

No MeSH data available.


Related in: MedlinePlus

Schematic diagrams depicting motifs and highly conserved residues within and between the RhtB (RB) and TerC (TC) families.A) Schematic diagram of RhtB proteins. B) Schematic diagram of TerC proteins. C) Graphical representation of the shared motifs depicted in Part A and Part B. D) Symbol Legend.
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pone.0137184.g006: Schematic diagrams depicting motifs and highly conserved residues within and between the RhtB (RB) and TerC (TC) families.A) Schematic diagram of RhtB proteins. B) Schematic diagram of TerC proteins. C) Graphical representation of the shared motifs depicted in Part A and Part B. D) Symbol Legend.

Mentions: The LysE superfamily consists of transmembrane transport proteins that catalyze export of amino acids, lipids and heavy metal ions. Statistical means were used to show that it includes newly identified families including transporters specific for (1) tellurium, (2) iron/lead, (3) manganese, (4) calcium, (5) nickel/cobalt, (6) amino acids, and (7) peptidoglycolipids as well as (8) one family of transmembrane electron carriers. Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication. Their common origin implies that they share common structural, mechanistic and functional attributes. The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations. They thus influence the physiology and pathogenesis of numerous microbes, being potential targets of drug action.


The LysE Superfamily of Transport Proteins Involved in Cell Physiology and Pathogenesis.

Tsu BV, Saier MH - PLoS ONE (2015)

Schematic diagrams depicting motifs and highly conserved residues within and between the RhtB (RB) and TerC (TC) families.A) Schematic diagram of RhtB proteins. B) Schematic diagram of TerC proteins. C) Graphical representation of the shared motifs depicted in Part A and Part B. D) Symbol Legend.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4608589&req=5

pone.0137184.g006: Schematic diagrams depicting motifs and highly conserved residues within and between the RhtB (RB) and TerC (TC) families.A) Schematic diagram of RhtB proteins. B) Schematic diagram of TerC proteins. C) Graphical representation of the shared motifs depicted in Part A and Part B. D) Symbol Legend.
Mentions: The LysE superfamily consists of transmembrane transport proteins that catalyze export of amino acids, lipids and heavy metal ions. Statistical means were used to show that it includes newly identified families including transporters specific for (1) tellurium, (2) iron/lead, (3) manganese, (4) calcium, (5) nickel/cobalt, (6) amino acids, and (7) peptidoglycolipids as well as (8) one family of transmembrane electron carriers. Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication. Their common origin implies that they share common structural, mechanistic and functional attributes. The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations. They thus influence the physiology and pathogenesis of numerous microbes, being potential targets of drug action.

Bottom Line: Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication.Their common origin implies that they share common structural, mechanistic and functional attributes.The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Biology, Division of Biological Sciences, University of California at San Diego, La Jolla, California, United States of America.

ABSTRACT
The LysE superfamily consists of transmembrane transport proteins that catalyze export of amino acids, lipids and heavy metal ions. Statistical means were used to show that it includes newly identified families including transporters specific for (1) tellurium, (2) iron/lead, (3) manganese, (4) calcium, (5) nickel/cobalt, (6) amino acids, and (7) peptidoglycolipids as well as (8) one family of transmembrane electron carriers. Internal repeats and conserved motifs were identified, and multiple alignments, phylogenetic trees and average hydropathy, amphipathicity and similarity plots provided evidence that all members of the superfamily derived from a single common 3-TMS precursor peptide via intragenic duplication. Their common origin implies that they share common structural, mechanistic and functional attributes. The transporters of this superfamily play important roles in ionic homeostasis, cell envelope assembly, and protection from excessive cytoplasmic heavy metal/metabolite concentrations. They thus influence the physiology and pathogenesis of numerous microbes, being potential targets of drug action.

No MeSH data available.


Related in: MedlinePlus