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Publication DateAnnual Review of Biochemistry, ISSN 0066-4154, 2008, Volume 77, Issue 1, pp. 643 - 667
About 25% to 30% of the bacterial proteins function in the cell envelope or outside of the cell. These proteins are synthesized in the cytosol, and the vast...
Membrane protein | Translocase | Proton motive force | Chaperone | SecA | SecY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-STRUCTURE | ESCHERICHIA-COLI SECA | PREPROTEIN TRANSLOCATION | proton motive force | chaperone | EXPORT CHAPERONE SECB | SIGNAL-RECOGNITION PARTICLE | DISTINCT ATP-BINDING | membrane protein | STOP-TRANSFER FUNCTION | PRECURSOR PROTEIN | translocase | Protein Structure, Tertiary | Protons | Bacteria - metabolism | Peptides - chemistry | Molecular Conformation | Bacterial Proteins - chemistry | Cytoplasm - metabolism | Molecular Chaperones - chemistry | Membrane Transport Proteins - chemistry | Protein Transport | SEC Translocation Channels | Models, Biological | Escherichia coli - metabolism | Adenosine Triphosphatases - chemistry | Cell Membrane - metabolism | Escherichia coli Proteins - chemistry | Proton-Motive Force | Chemical properties | Ribosomal proteins | Translocation (Genetics) | Structure | Analysis | Membrane proteins
Membrane protein | Translocase | Proton motive force | Chaperone | SecA | SecY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-STRUCTURE | ESCHERICHIA-COLI SECA | PREPROTEIN TRANSLOCATION | proton motive force | chaperone | EXPORT CHAPERONE SECB | SIGNAL-RECOGNITION PARTICLE | DISTINCT ATP-BINDING | membrane protein | STOP-TRANSFER FUNCTION | PRECURSOR PROTEIN | translocase | Protein Structure, Tertiary | Protons | Bacteria - metabolism | Peptides - chemistry | Molecular Conformation | Bacterial Proteins - chemistry | Cytoplasm - metabolism | Molecular Chaperones - chemistry | Membrane Transport Proteins - chemistry | Protein Transport | SEC Translocation Channels | Models, Biological | Escherichia coli - metabolism | Adenosine Triphosphatases - chemistry | Cell Membrane - metabolism | Escherichia coli Proteins - chemistry | Proton-Motive Force | Chemical properties | Ribosomal proteins | Translocation (Genetics) | Structure | Analysis | Membrane proteins
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Loading RightsMolecular Microbiology, ISSN 0950-382X, 05/2011, Volume 80, Issue 3, pp. 588 - 595
The essential cellular functions of secretion and protein degradation require a molecular machine to unfold and translocate proteins either across a membrane...
COMPLEX | CHANNEL | MECHANISM | LETHAL FACTOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PORE | PROTEIN-TRANSLOCATION | MICROBIOLOGY | BINDING | PEPTIDE | PHENYLALANINE CLAMP | Bacterial Toxins - metabolism | Protein Multimerization | Cell Membrane - metabolism | Antigens, Bacterial - metabolism | Protein Folding | Protein Subunits - metabolism | Protein Transport | Antigens | Enzymes | Anthrax | Proteolysis | Analysis | Index Medicus | protein unfolding | proton gradient | Brownian ratchet | nonspecific binding | protein translocation
COMPLEX | CHANNEL | MECHANISM | LETHAL FACTOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PORE | PROTEIN-TRANSLOCATION | MICROBIOLOGY | BINDING | PEPTIDE | PHENYLALANINE CLAMP | Bacterial Toxins - metabolism | Protein Multimerization | Cell Membrane - metabolism | Antigens, Bacterial - metabolism | Protein Folding | Protein Subunits - metabolism | Protein Transport | Antigens | Enzymes | Anthrax | Proteolysis | Analysis | Index Medicus | protein unfolding | proton gradient | Brownian ratchet | nonspecific binding | protein translocation
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Loading RightsBBA - Molecular Cell Research, ISSN 0167-4889, 10/2015, Volume 1853, Issue 10, pp. 2745 - 2753
The twin-arginine translocation system (Tat) is a protein transport system that moves fully folded and cofactor-containing proteins across membranes of...
TatAc | Twin-arginine translocation | TatB | Bacillus subtilis | TatA | EfeB | TRANSPORT SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | EXPORT | SUBUNITS | SIGNAL PEPTIDE | CELL BIOLOGY | GRAM-POSITIVE BACTERIA | PATHWAY | FOLDED PROTEINS | SECRETION | PROTON GRADIENT | Proteins | Arginine | Life Sciences | Other
TatAc | Twin-arginine translocation | TatB | Bacillus subtilis | TatA | EfeB | TRANSPORT SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | EXPORT | SUBUNITS | SIGNAL PEPTIDE | CELL BIOLOGY | GRAM-POSITIVE BACTERIA | PATHWAY | FOLDED PROTEINS | SECRETION | PROTON GRADIENT | Proteins | Arginine | Life Sciences | Other
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Loading RightsAnnual Review of Biochemistry, ISSN 0066-4154, 6/2015, Volume 84, Issue 1, pp. 843 - 864
The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and some mitochondria, allows folded proteins to be moved across membranes....
protein transport | signal peptide | bacterial protein export | membrane protein | thylakoid import | twin-arginine | Signal peptide | Membrane protein | Bacterial protein export | Protein transport | Thylakoid import | Twin-arginine | Archaea - metabolism | Bacteria - metabolism | Prokaryotic Cells - metabolism | Twin-Arginine-Translocation System - metabolism | Bacteria - classification | Twin-Arginine-Translocation System - chemistry | Mitochondria - metabolism | Archaea - classification | Chloroplasts - metabolism | Protein Transport | Proton-Motive Force | Proteins | Arginine | Translocation (Genetics) | Health aspects | Identification and classification | Protein-protein interactions
protein transport | signal peptide | bacterial protein export | membrane protein | thylakoid import | twin-arginine | Signal peptide | Membrane protein | Bacterial protein export | Protein transport | Thylakoid import | Twin-arginine | Archaea - metabolism | Bacteria - metabolism | Prokaryotic Cells - metabolism | Twin-Arginine-Translocation System - metabolism | Bacteria - classification | Twin-Arginine-Translocation System - chemistry | Mitochondria - metabolism | Archaea - classification | Chloroplasts - metabolism | Protein Transport | Proton-Motive Force | Proteins | Arginine | Translocation (Genetics) | Health aspects | Identification and classification | Protein-protein interactions
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Loading RightsMolecular Aspects of Medicine, ISSN 0098-2997, 2009, Volume 30, Issue 6, pp. 413 - 422
Much attention has been focused on anthrax toxin recently, both because of its central role in the pathogenesis of and because it has proven to be one of the...
Planar bilayer | Brownian ratchet | Proton gradient | MEDICINE, RESEARCH & EXPERIMENTAL | ACTION IN-VIVO | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CAPILLARY MORPHOGENESIS PROTEIN-2 | EDEMA FACTOR | TRANSMEMBRANE PORE | DIPHTHERIA-TOXIN | HEPTAMERIC PROTECTIVE ANTIGEN | LETHAL FACTOR | BACILLUS-ANTHRACIS | PHENYLALANINE CLAMP | Protein Structure, Tertiary | Antigens, Bacterial - chemistry | Phenylalanine - metabolism | Bacillus anthracis - pathogenicity | Models, Molecular | Protein Transport - physiology | Antigens, Bacterial - genetics | Anthrax - microbiology | Bacterial Toxins - chemistry | Protein Subunits - metabolism | Endocytosis - physiology | Bacterial Toxins - metabolism | Animals | Protein Structure, Quaternary | Bacterial Toxins - genetics | Cell Membrane - metabolism | Protein Subunits - chemistry | Mutation | Bacillus anthracis - genetics | Antigens, Bacterial - metabolism | Bacillus anthracis - metabolism | Hydrogen-Ion Concentration | Protein Subunits - genetics | proton gradient | planar bilayer
Planar bilayer | Brownian ratchet | Proton gradient | MEDICINE, RESEARCH & EXPERIMENTAL | ACTION IN-VIVO | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CAPILLARY MORPHOGENESIS PROTEIN-2 | EDEMA FACTOR | TRANSMEMBRANE PORE | DIPHTHERIA-TOXIN | HEPTAMERIC PROTECTIVE ANTIGEN | LETHAL FACTOR | BACILLUS-ANTHRACIS | PHENYLALANINE CLAMP | Protein Structure, Tertiary | Antigens, Bacterial - chemistry | Phenylalanine - metabolism | Bacillus anthracis - pathogenicity | Models, Molecular | Protein Transport - physiology | Antigens, Bacterial - genetics | Anthrax - microbiology | Bacterial Toxins - chemistry | Protein Subunits - metabolism | Endocytosis - physiology | Bacterial Toxins - metabolism | Animals | Protein Structure, Quaternary | Bacterial Toxins - genetics | Cell Membrane - metabolism | Protein Subunits - chemistry | Mutation | Bacillus anthracis - genetics | Antigens, Bacterial - metabolism | Bacillus anthracis - metabolism | Hydrogen-Ion Concentration | Protein Subunits - genetics | proton gradient | planar bilayer
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Loading RightsNature, ISSN 0028-0836, 08/2012, Volume 488, Issue 7412, pp. 531 - 534
In plants, transport processes are important for the reallocation of defence compounds to protect tissues of high value(1), as demonstrated in the plant model...
FIBER | ARABIDOPSIS-THALIANA | NITRATE | PRODUCTS | PATHWAY | CLONING | MULTIDISCIPLINARY SCIENCES | GROWTH | ACCUMULATION | PHLOEM | FOOD | Protons | Arabidopsis Proteins - genetics | Monosaccharide Transport Proteins - deficiency | Seeds - metabolism | Gene Library | Oocytes - metabolism | Xenopus laevis | Arabidopsis - embryology | Cell Extracts - chemistry | Glucosinolates - metabolism | Organ Specificity | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Animals | Glucosinolates - pharmacology | Genes, Plant - genetics | Gene Deletion | Phloem - metabolism | Oocytes - drug effects | Biological Transport - drug effects | Monosaccharide Transport Proteins - metabolism | Evolution, Molecular | Monosaccharide Transport Proteins - genetics | Physiological aspects | Seeds | Research | Translocation (Genetics) | Carrier proteins | Proteins | Phylogenetics | Nitrates | Metabolites | Biological & chemical weapons
FIBER | ARABIDOPSIS-THALIANA | NITRATE | PRODUCTS | PATHWAY | CLONING | MULTIDISCIPLINARY SCIENCES | GROWTH | ACCUMULATION | PHLOEM | FOOD | Protons | Arabidopsis Proteins - genetics | Monosaccharide Transport Proteins - deficiency | Seeds - metabolism | Gene Library | Oocytes - metabolism | Xenopus laevis | Arabidopsis - embryology | Cell Extracts - chemistry | Glucosinolates - metabolism | Organ Specificity | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Animals | Glucosinolates - pharmacology | Genes, Plant - genetics | Gene Deletion | Phloem - metabolism | Oocytes - drug effects | Biological Transport - drug effects | Monosaccharide Transport Proteins - metabolism | Evolution, Molecular | Monosaccharide Transport Proteins - genetics | Physiological aspects | Seeds | Research | Translocation (Genetics) | Carrier proteins | Proteins | Phylogenetics | Nitrates | Metabolites | Biological & chemical weapons
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Loading RightsJournal of Chemical Physics, ISSN 0021-9606, 07/2010, Volume 133, Issue 4, pp. 045101 - 045101-12
We have measured the ionic current blockages produced by single molecules of sodium poly(styrene sulfonate) passing through an α -hemolysin protein pore under...
TRANSPORT | DNA HAIRPIN MOLECULES | DISCRIMINATION | ORIENTATION | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | RNA MOLECULES | ION-CHANNEL | TRANSMEMBRANE PORE | POLYNUCLEOTIDE MOLECULES | MEMBRANE CHANNEL | NANOPORE | Models, Theoretical | Protons | Probability | Entropy | Hemolysin Proteins - chemistry | Static Electricity | Algorithms | Biological Transport | Stochastic Processes | Polymers - chemistry | Porosity | Hemolysin Proteins - metabolism | Polymers - metabolism | Hydrogen-Ion Concentration | Biological Molecules, Biopolymers, and Biological Systems
TRANSPORT | DNA HAIRPIN MOLECULES | DISCRIMINATION | ORIENTATION | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | RNA MOLECULES | ION-CHANNEL | TRANSMEMBRANE PORE | POLYNUCLEOTIDE MOLECULES | MEMBRANE CHANNEL | NANOPORE | Models, Theoretical | Protons | Probability | Entropy | Hemolysin Proteins - chemistry | Static Electricity | Algorithms | Biological Transport | Stochastic Processes | Polymers - chemistry | Porosity | Hemolysin Proteins - metabolism | Polymers - metabolism | Hydrogen-Ion Concentration | Biological Molecules, Biopolymers, and Biological Systems
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Loading RightsMolecular Cell, ISSN 1097-2765, 2000, Volume 6, Issue 6, pp. 1425 - 1436
The association of actin filaments with the plasma membrane maintains cell shape and adhesion. Here, we show that the plasma membrane ion exchanger NHE1 acts...
CYTOPLASMIC DOMAIN | TERMINAL DOMAINS | F-ACTIN BINDING | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | EZRIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | INTRACELLULAR PH | FAMILY MEMBERS | NA+/H+ EXCHANGER | BAND-3 PROTEIN | CELL BIOLOGY | Protons | Humans | Molecular Sequence Data | Blood Proteins - metabolism | Phosphoproteins - metabolism | Recombinant Fusion Proteins - metabolism | Sodium-Hydrogen Exchangers - metabolism | DNA-Binding Proteins - metabolism | Cell Division | Cytoskeletal Proteins - metabolism | Sodium-Hydrogen Exchangers - genetics | Ion Transport | Membrane Proteins - metabolism | Hydrogen - metabolism | Amino Acid Sequence | Cell Line | Cell Size | Precipitin Tests | Transcription Factors - metabolism | Sodium-Hydrogen Exchangers - chemistry | Sequence Alignment | Stress Fibers - metabolism | Animals | Focal Adhesions - metabolism | Cytoskeleton - metabolism | Protein Binding | Mutation | Microscopy, Fluorescence
CYTOPLASMIC DOMAIN | TERMINAL DOMAINS | F-ACTIN BINDING | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | EZRIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | INTRACELLULAR PH | FAMILY MEMBERS | NA+/H+ EXCHANGER | BAND-3 PROTEIN | CELL BIOLOGY | Protons | Humans | Molecular Sequence Data | Blood Proteins - metabolism | Phosphoproteins - metabolism | Recombinant Fusion Proteins - metabolism | Sodium-Hydrogen Exchangers - metabolism | DNA-Binding Proteins - metabolism | Cell Division | Cytoskeletal Proteins - metabolism | Sodium-Hydrogen Exchangers - genetics | Ion Transport | Membrane Proteins - metabolism | Hydrogen - metabolism | Amino Acid Sequence | Cell Line | Cell Size | Precipitin Tests | Transcription Factors - metabolism | Sodium-Hydrogen Exchangers - chemistry | Sequence Alignment | Stress Fibers - metabolism | Animals | Focal Adhesions - metabolism | Cytoskeleton - metabolism | Protein Binding | Mutation | Microscopy, Fluorescence
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Loading RightsProceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2012, Volume 109, Issue 3, pp. 947 - 952
ATP synthases are the primary source of ATP in all living cells. To catalyze ATP synthesis, these membrane-associated complexes use a rotary mechanism powered...
Hydrolysis | Oligomers | Protons | Enzymes | Sodium | Archaea | Adenosine triphosphatases | Ions | Modeling | Binding sites | Energetic limit | Energy conservation | Ion specificity | ATPase | Methanogens | ACETOBACTERIUM-WOODII | ROTARY MECHANISM | ENTEROCOCCUS-HIRAE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ion specificity | PROPIONIGENIUM-MODESTUM | methanogens | C SUBUNIT OLIGOMER | AA(o) ATPase | METHANOGENIC ARCHAEA | energy conservation | energetic limit | PROTEOLIPID RING | BINDING-SITE | AQUEOUS ACCESS | Methanosarcina - enzymology | Adenosine Triphosphatases - metabolism | Sodium - metabolism | Protein Subunits - metabolism | Unilamellar Liposomes - metabolism | Biological Transport | Energy Metabolism | Models, Biological | Adenosine Triphosphate - metabolism | Protein Binding | Hydrogen-Ion Concentration | Biological Sciences | A1Ao ATPase
Hydrolysis | Oligomers | Protons | Enzymes | Sodium | Archaea | Adenosine triphosphatases | Ions | Modeling | Binding sites | Energetic limit | Energy conservation | Ion specificity | ATPase | Methanogens | ACETOBACTERIUM-WOODII | ROTARY MECHANISM | ENTEROCOCCUS-HIRAE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ion specificity | PROPIONIGENIUM-MODESTUM | methanogens | C SUBUNIT OLIGOMER | AA(o) ATPase | METHANOGENIC ARCHAEA | energy conservation | energetic limit | PROTEOLIPID RING | BINDING-SITE | AQUEOUS ACCESS | Methanosarcina - enzymology | Adenosine Triphosphatases - metabolism | Sodium - metabolism | Protein Subunits - metabolism | Unilamellar Liposomes - metabolism | Biological Transport | Energy Metabolism | Models, Biological | Adenosine Triphosphate - metabolism | Protein Binding | Hydrogen-Ion Concentration | Biological Sciences | A1Ao ATPase
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