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Publication DateNature, ISSN 0028-0836, 08/2015, Volume 524, Issue 7563, pp. 119 - 124
The ribosome is a ribonucleoprotein machine responsible for protein synthesis. In all kingdoms of life it is composed of two subunits, each built on its own...
EXIT TUNNEL | SITE | PEPTIDYL-TRANSFERASE CENTER | RNA | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | TRANSCRIPTION | PURIFIED COMPONENTS | MUTATIONS | INHIBITORS | TRANSLATION | Amino Acid Sequence | Peptidyl Transferases - metabolism | Peptidyl Transferases - genetics | Molecular Conformation | Peptidyl Transferases - chemistry | RNA, Messenger - genetics | Ribosomes - chemistry | Models, Molecular | Ribosomes - metabolism | Escherichia coli - cytology | Mutation - genetics | RNA, Messenger - metabolism | Protein Subunits - metabolism | Bioengineering - methods | RNA, Ribosomal, 23S - genetics | Ribosomes - genetics | Escherichia coli - genetics | Base Sequence | Escherichia coli - metabolism | Protein Biosynthesis - genetics | Protein Subunits - chemistry | Escherichia coli - growth & development | RNA, Ribosomal, 23S - metabolism | Protein biosynthesis | Genetic translation | Analysis | Ribosomes | Proteins | Peptides | Protein synthesis | Lymphocytes | Cloning | Genomes | Mutation | Gene expression | Ribonucleic acid--RNA
EXIT TUNNEL | SITE | PEPTIDYL-TRANSFERASE CENTER | RNA | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | TRANSCRIPTION | PURIFIED COMPONENTS | MUTATIONS | INHIBITORS | TRANSLATION | Amino Acid Sequence | Peptidyl Transferases - metabolism | Peptidyl Transferases - genetics | Molecular Conformation | Peptidyl Transferases - chemistry | RNA, Messenger - genetics | Ribosomes - chemistry | Models, Molecular | Ribosomes - metabolism | Escherichia coli - cytology | Mutation - genetics | RNA, Messenger - metabolism | Protein Subunits - metabolism | Bioengineering - methods | RNA, Ribosomal, 23S - genetics | Ribosomes - genetics | Escherichia coli - genetics | Base Sequence | Escherichia coli - metabolism | Protein Biosynthesis - genetics | Protein Subunits - chemistry | Escherichia coli - growth & development | RNA, Ribosomal, 23S - metabolism | Protein biosynthesis | Genetic translation | Analysis | Ribosomes | Proteins | Peptides | Protein synthesis | Lymphocytes | Cloning | Genomes | Mutation | Gene expression | Ribonucleic acid--RNA
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Loading RightsTrends in Biochemical Sciences, ISSN 0968-0004, 08/2017, Volume 42, Issue 8, pp. 640 - 654
The biogenesis of eukaryotic ribosomes is a complicated process during which the transcription, modification, folding, and processing of the rRNA is coupled...
preribosomal particles | ribosomopathy | cryoelectron microscopy | quality control | rRNA processing | ribosome biogenesis | NUCLEAR-EXPORT FACTOR | AAA-ATPASE DRG1 | ASSEMBLY FACTORS | EUKARYOTIC RIBOSOME | BIOGENESIS FACTORS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PRE-40S RIBOSOMES | TRANSLATION INITIATION | QUALITY-CONTROL | SACCHAROMYCES-CEREVISIAE | Cryoelectron Microscopy | Ribosomes - genetics | Ribosomes - chemistry | Ribosomes - metabolism | Protein Subunits - chemistry | Nucleic Acid Conformation | Protein Subunits - metabolism | Protein Subunits - genetics | Proteins | RNA
preribosomal particles | ribosomopathy | cryoelectron microscopy | quality control | rRNA processing | ribosome biogenesis | NUCLEAR-EXPORT FACTOR | AAA-ATPASE DRG1 | ASSEMBLY FACTORS | EUKARYOTIC RIBOSOME | BIOGENESIS FACTORS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PRE-40S RIBOSOMES | TRANSLATION INITIATION | QUALITY-CONTROL | SACCHAROMYCES-CEREVISIAE | Cryoelectron Microscopy | Ribosomes - genetics | Ribosomes - chemistry | Ribosomes - metabolism | Protein Subunits - chemistry | Nucleic Acid Conformation | Protein Subunits - metabolism | Protein Subunits - genetics | Proteins | RNA
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Loading RightsJournal of Cell Biology, ISSN 0021-9525, 03/2016, Volume 212, Issue 7, pp. 845 - 860
Mammalian stress granules (SGs) contain stalled translation preinitiation complexes that are assembled into discrete granules by specific RNA-binding proteins...
Phosphorylation | Humans | Cercopithecus aethiops | Molecular Sequence Data | Microscopy, Video | Structure-Activity Relationship | Ribosomal Proteins - metabolism | Poly-ADP-Ribose Binding Proteins | Cytoplasmic Granules - enzymology | RNA Helicases | Transfection | RNA Interference | Base Sequence | Cell Cycle Proteins - genetics | Eukaryotic Initiation Factor-2 - metabolism | Ubiquitin Thiolesterase - metabolism | Protein Interaction Domains and Motifs | RNA Recognition Motif Proteins | Ribosome Subunits, Small, Eukaryotic - genetics | Amino Acid Sequence | Signal Transduction | Ribosomal Proteins - genetics | Cell Cycle Proteins - metabolism | Ubiquitin Thiolesterase - genetics | Carrier Proteins - genetics | Microscopy, Confocal | DNA Helicases | Animals | Carrier Proteins - metabolism | Cytoplasmic Granules - genetics | Cell Line, Tumor | Protein Binding | Protein Conformation | Mutation | Eukaryotic Initiation Factor-4A - metabolism | Ribosome Subunits, Small, Eukaryotic - metabolism | COS Cells
Phosphorylation | Humans | Cercopithecus aethiops | Molecular Sequence Data | Microscopy, Video | Structure-Activity Relationship | Ribosomal Proteins - metabolism | Poly-ADP-Ribose Binding Proteins | Cytoplasmic Granules - enzymology | RNA Helicases | Transfection | RNA Interference | Base Sequence | Cell Cycle Proteins - genetics | Eukaryotic Initiation Factor-2 - metabolism | Ubiquitin Thiolesterase - metabolism | Protein Interaction Domains and Motifs | RNA Recognition Motif Proteins | Ribosome Subunits, Small, Eukaryotic - genetics | Amino Acid Sequence | Signal Transduction | Ribosomal Proteins - genetics | Cell Cycle Proteins - metabolism | Ubiquitin Thiolesterase - genetics | Carrier Proteins - genetics | Microscopy, Confocal | DNA Helicases | Animals | Carrier Proteins - metabolism | Cytoplasmic Granules - genetics | Cell Line, Tumor | Protein Binding | Protein Conformation | Mutation | Eukaryotic Initiation Factor-4A - metabolism | Ribosome Subunits, Small, Eukaryotic - metabolism | COS Cells
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Loading RightsCell, ISSN 0092-8674, 2001, Volume 107, Issue 3, pp. 373 - 386
A cryo-EM reconstruction of the translating yeast 80S ribosome was analyzed. Computationally separated rRNA and protein densities were used for docking of...
P-SITE | ANGSTROM RESOLUTION | DENSITY MAPS | CRYOELECTRON MICROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 30 S | A-SITE | COLI 70S RIBOSOME | TRANSFER-RNA | PSI-BLAST | EXPANSION SEGMENTS | CELL BIOLOGY | RNA, Ribosomal, 5.8S - chemistry | RNA | RNA, Transfer - metabolism | Saccharomyces cerevisiae - genetics | RNA, Fungal - chemistry | RNA, Ribosomal - chemistry | Models, Molecular | Molecular Sequence Data | Ribosomes - metabolism | RNA, Fungal - metabolism | RNA, Ribosomal, 18S - chemistry | Ribosomes - ultrastructure | Base Sequence | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | Cryoelectron Microscopy - methods | Molecular structure | Analysis | Ribosomes | Models | Saccharomyces | Research | Structure | Structure-activity relationships (Biochemistry)
P-SITE | ANGSTROM RESOLUTION | DENSITY MAPS | CRYOELECTRON MICROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 30 S | A-SITE | COLI 70S RIBOSOME | TRANSFER-RNA | PSI-BLAST | EXPANSION SEGMENTS | CELL BIOLOGY | RNA, Ribosomal, 5.8S - chemistry | RNA | RNA, Transfer - metabolism | Saccharomyces cerevisiae - genetics | RNA, Fungal - chemistry | RNA, Ribosomal - chemistry | Models, Molecular | Molecular Sequence Data | Ribosomes - metabolism | RNA, Fungal - metabolism | RNA, Ribosomal, 18S - chemistry | Ribosomes - ultrastructure | Base Sequence | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | Cryoelectron Microscopy - methods | Molecular structure | Analysis | Ribosomes | Models | Saccharomyces | Research | Structure | Structure-activity relationships (Biochemistry)
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Loading RightsCurrent Opinion in Structural Biology, ISSN 0959-440X, 04/2018, Volume 49, pp. 85 - 93
The small subunit processome is the first precursor of the small eukaryotic ribosomal subunit. During its assembly in the nucleolus, many ribosome biogenesis...
INTERACTION NETWORK | 90S PRERIBOSOME | YEAST | RNA | EUKARYOTIC RIBOSOME | BIOCHEMISTRY & MOLECULAR BIOLOGY | PRE-RIBOSOMES | EARLY CLEAVAGE | SACCHAROMYCES-CEREVISIAE | U3 SNORNA | PIN DOMAIN | CELL BIOLOGY | RNA Precursors - chemistry | Ribosomal Proteins - chemistry | Humans | RNA, Ribosomal - chemistry | Models, Molecular | RNA, Ribosomal - metabolism | Ribosome Subunits, Small - chemistry | Ribosomal Proteins - metabolism | Ribosome Subunits, Small - metabolism | Animals | Protein Conformation | RNA Precursors - metabolism | Nucleic Acid Conformation | Proteins | Ribosomal RNA
INTERACTION NETWORK | 90S PRERIBOSOME | YEAST | RNA | EUKARYOTIC RIBOSOME | BIOCHEMISTRY & MOLECULAR BIOLOGY | PRE-RIBOSOMES | EARLY CLEAVAGE | SACCHAROMYCES-CEREVISIAE | U3 SNORNA | PIN DOMAIN | CELL BIOLOGY | RNA Precursors - chemistry | Ribosomal Proteins - chemistry | Humans | RNA, Ribosomal - chemistry | Models, Molecular | RNA, Ribosomal - metabolism | Ribosome Subunits, Small - chemistry | Ribosomal Proteins - metabolism | Ribosome Subunits, Small - metabolism | Animals | Protein Conformation | RNA Precursors - metabolism | Nucleic Acid Conformation | Proteins | Ribosomal RNA
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Loading RightsScience, ISSN 0036-8075, 01/2015, Volume 347, Issue 6217, pp. 75 - 78
In Eukarya, stalled translation induces 40S dissociation and recruitment of the ribosome quality control complex (RQC) to the 60S subunit, which mediates...
Saccharomyces cerevisiae Proteins - ultrastructure | Ribosome Subunits, Large, Eukaryotic - ultrastructure | RNA, Transfer, Thr - metabolism | Ribosome Subunits, Large, Eukaryotic - chemistry | Saccharomyces cerevisiae - genetics | Peptide Biosynthesis, Nucleic Acid-Independent | Ubiquitin-Protein Ligases - metabolism | RNA-Binding Proteins | RNA, Messenger - metabolism | RNA, Transfer, Ala - metabolism | Ubiquitin-Protein Ligases - ultrastructure | RNA, Transfer, Thr - chemistry | Cryoelectron Microscopy | Saccharomyces cerevisiae - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Conformation | RNA, Transfer, Ala - chemistry | Nucleic Acid Conformation
Saccharomyces cerevisiae Proteins - ultrastructure | Ribosome Subunits, Large, Eukaryotic - ultrastructure | RNA, Transfer, Thr - metabolism | Ribosome Subunits, Large, Eukaryotic - chemistry | Saccharomyces cerevisiae - genetics | Peptide Biosynthesis, Nucleic Acid-Independent | Ubiquitin-Protein Ligases - metabolism | RNA-Binding Proteins | RNA, Messenger - metabolism | RNA, Transfer, Ala - metabolism | Ubiquitin-Protein Ligases - ultrastructure | RNA, Transfer, Thr - chemistry | Cryoelectron Microscopy | Saccharomyces cerevisiae - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Conformation | RNA, Transfer, Ala - chemistry | Nucleic Acid Conformation
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Loading RightsScience, ISSN 0036-8075, 01/2017, Volume 355, Issue 6321, pp. eaal1880 - eaal1880
The small subunit (SSU) processome, a large ribonucleoprotein particle, organizes the assembly of the eukaryotic small ribosomal subunit by coordinating the...
ASSEMBLY FACTOR | PROTEIN | BIOGENESIS | EUKARYOTIC RIBOSOME | MULTIDISCIPLINARY SCIENCES | IN-VIVO | PRE-RIBOSOMAL-RNA | EXTERNAL TRANSCRIBED SPACER | U3 SNORNA | SMALL NUCLEOLAR RNA | PEPTIDE | Saccharomyces cerevisiae Proteins - ultrastructure | RNA, Fungal - ultrastructure | Ribosome Subunits, Small, Eukaryotic - chemistry | RNA, Fungal - chemistry | RNA, Ribosomal - chemistry | Ribosome Subunits, Small, Eukaryotic - ultrastructure | Saccharomyces cerevisiae - ultrastructure | RNA, Ribosomal, 18S - ultrastructure | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | RNA, Ribosomal - ultrastructure | RNA, Ribosomal, 18S - chemistry | RNA, Small Nucleolar - chemistry | RNA, Small Nucleolar - ultrastructure | Protein Conformation, beta-Strand | Nucleic Acid Conformation | Saccharomyces cerevisiae Proteins - chemistry | RNA modification | Enzymes | Construction | Yeast | Transcription | snoRNA U3 | rRNA 35S | Guanosine | Spatial discrimination | Ribosomal DNA | Color | Biosynthesis | Electron microscopy | snoRNA | Recruitment | Proteins | Nucleoli | Triphosphatase | Spacer | Cleavage | rRNA 18S | Molecular structure | Maturation | Ribonucleic acids | Molecular motors | Spacers | Assembly
ASSEMBLY FACTOR | PROTEIN | BIOGENESIS | EUKARYOTIC RIBOSOME | MULTIDISCIPLINARY SCIENCES | IN-VIVO | PRE-RIBOSOMAL-RNA | EXTERNAL TRANSCRIBED SPACER | U3 SNORNA | SMALL NUCLEOLAR RNA | PEPTIDE | Saccharomyces cerevisiae Proteins - ultrastructure | RNA, Fungal - ultrastructure | Ribosome Subunits, Small, Eukaryotic - chemistry | RNA, Fungal - chemistry | RNA, Ribosomal - chemistry | Ribosome Subunits, Small, Eukaryotic - ultrastructure | Saccharomyces cerevisiae - ultrastructure | RNA, Ribosomal, 18S - ultrastructure | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | RNA, Ribosomal - ultrastructure | RNA, Ribosomal, 18S - chemistry | RNA, Small Nucleolar - chemistry | RNA, Small Nucleolar - ultrastructure | Protein Conformation, beta-Strand | Nucleic Acid Conformation | Saccharomyces cerevisiae Proteins - chemistry | RNA modification | Enzymes | Construction | Yeast | Transcription | snoRNA U3 | rRNA 35S | Guanosine | Spatial discrimination | Ribosomal DNA | Color | Biosynthesis | Electron microscopy | snoRNA | Recruitment | Proteins | Nucleoli | Triphosphatase | Spacer | Cleavage | rRNA 18S | Molecular structure | Maturation | Ribonucleic acids | Molecular motors | Spacers | Assembly
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Loading RightsScience, ISSN 0036-8075, 5/2001, Volume 292, Issue 5518, pp. 897 - 902
Crystal structures of the 30S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the...
Messenger RNA | Hydrogen bonds | RNA | Antibiotics | Protein synthesis | Ribosomes | Crystals | Research Articles | Codons | Anticodon | Transfer RNA | P-SITE | ANGSTROM RESOLUTION | ELONGATION-FACTOR TU | ESCHERICHIA-COLI RIBOSOME | AMINOACYL-TRANSFER-RNA | PHENYLALANINE TRANSFER-RNA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | A-SITE | 70S RIBOSOME | DNA-REPLICATION | Codon - metabolism | Anticodon - metabolism | Protein Biosynthesis | Peptide Chain Elongation, Translational | RNA, Transfer, Phe - chemistry | Anticodon - chemistry | RNA, Transfer, Amino Acid-Specific - metabolism | Ribosomes - metabolism | Thermus thermophilus - metabolism | Crystallography, X-Ray | Thermus thermophilus - ultrastructure | Guanosine Triphosphate - metabolism | RNA, Messenger - metabolism | Paromomycin - pharmacology | Thermodynamics | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | RNA, Bacterial - metabolism | RNA, Ribosomal, 16S - metabolism | RNA, Transfer, Phe - metabolism | Thermus thermophilus - chemistry | RNA, Transfer - metabolism | Ribosomes - chemistry | Models, Molecular | Anti-Bacterial Agents - metabolism | Peptide Elongation Factor Tu - metabolism | RNA, Transfer, Amino Acid-Specific - chemistry | RNA, Ribosomal, 16S - chemistry | Ribosomes - ultrastructure | Codon - chemistry | Base Pairing | Hydrogen Bonding | RNA, Bacterial - chemistry | RNA, Messenger - chemistry | Anti-Bacterial Agents - pharmacology | Paromomycin - metabolism | Protein research | Usage | Polypeptides | Amino acids | Research | Molecular biology | Statistics | Ribonucleic acid--RNA | Ribonucleic acid
Messenger RNA | Hydrogen bonds | RNA | Antibiotics | Protein synthesis | Ribosomes | Crystals | Research Articles | Codons | Anticodon | Transfer RNA | P-SITE | ANGSTROM RESOLUTION | ELONGATION-FACTOR TU | ESCHERICHIA-COLI RIBOSOME | AMINOACYL-TRANSFER-RNA | PHENYLALANINE TRANSFER-RNA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | A-SITE | 70S RIBOSOME | DNA-REPLICATION | Codon - metabolism | Anticodon - metabolism | Protein Biosynthesis | Peptide Chain Elongation, Translational | RNA, Transfer, Phe - chemistry | Anticodon - chemistry | RNA, Transfer, Amino Acid-Specific - metabolism | Ribosomes - metabolism | Thermus thermophilus - metabolism | Crystallography, X-Ray | Thermus thermophilus - ultrastructure | Guanosine Triphosphate - metabolism | RNA, Messenger - metabolism | Paromomycin - pharmacology | Thermodynamics | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | RNA, Bacterial - metabolism | RNA, Ribosomal, 16S - metabolism | RNA, Transfer, Phe - metabolism | Thermus thermophilus - chemistry | RNA, Transfer - metabolism | Ribosomes - chemistry | Models, Molecular | Anti-Bacterial Agents - metabolism | Peptide Elongation Factor Tu - metabolism | RNA, Transfer, Amino Acid-Specific - chemistry | RNA, Ribosomal, 16S - chemistry | Ribosomes - ultrastructure | Codon - chemistry | Base Pairing | Hydrogen Bonding | RNA, Bacterial - chemistry | RNA, Messenger - chemistry | Anti-Bacterial Agents - pharmacology | Paromomycin - metabolism | Protein research | Usage | Polypeptides | Amino acids | Research | Molecular biology | Statistics | Ribonucleic acid--RNA | Ribonucleic acid
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Loading RightsMolecular Ecology, ISSN 0962-1083, 06/2016, Volume 25, Issue 12, pp. 2816 - 2832
Arbuscular mycorrhizal (AM) fungi are known to exhibit high intra‐organism genetic variation. However, information about intra‐ vs. interspecific variation...
qiime | arbuscular mycorrhizal fungi | sequence‐based identification | rDNA variation | Sequence-based identification | Arbuscular mycorrhizal fungi | RDNA variation | sequence-based identification | SPECIES LEVEL | RNA GENES | GLOMEROMYCOTA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENVIRONMENTAL SEQUENCES | IDENTIFICATION | MOLECULAR DIVERSITY | GENETIC-VARIATION | EVOLUTIONARY BIOLOGY | GLOMUS-INTRARADICES | COMMUNITY | ECOLOGY | QIIME | Genetic Variation | Ribosome Subunits, Small - genetics | Mycorrhizae - genetics | DNA, Fungal - genetics | DNA, Ribosomal Spacer - genetics | Glomeromycota - classification | Ribosome Subunits, Large - genetics | Glomeromycota - genetics | High-Throughput Nucleotide Sequencing | Polymorphism, Single Nucleotide | Sequence Analysis, DNA | Single nucleotide polymorphisms | Nucleotide sequencing | Ribosomal RNA | Chromosomes | DNA sequencing | Fungi | Genetic diversity | Molecular biology | Taxonomy | Polymorphism
qiime | arbuscular mycorrhizal fungi | sequence‐based identification | rDNA variation | Sequence-based identification | Arbuscular mycorrhizal fungi | RDNA variation | sequence-based identification | SPECIES LEVEL | RNA GENES | GLOMEROMYCOTA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENVIRONMENTAL SEQUENCES | IDENTIFICATION | MOLECULAR DIVERSITY | GENETIC-VARIATION | EVOLUTIONARY BIOLOGY | GLOMUS-INTRARADICES | COMMUNITY | ECOLOGY | QIIME | Genetic Variation | Ribosome Subunits, Small - genetics | Mycorrhizae - genetics | DNA, Fungal - genetics | DNA, Ribosomal Spacer - genetics | Glomeromycota - classification | Ribosome Subunits, Large - genetics | Glomeromycota - genetics | High-Throughput Nucleotide Sequencing | Polymorphism, Single Nucleotide | Sequence Analysis, DNA | Single nucleotide polymorphisms | Nucleotide sequencing | Ribosomal RNA | Chromosomes | DNA sequencing | Fungi | Genetic diversity | Molecular biology | Taxonomy | Polymorphism
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Loading RightsMolecular Microbiology, ISSN 0950-382X, 09/2012, Volume 85, Issue 6, pp. 1194 - 1203
Summary The binding site of the cyclic peptide antibiotics capreomycin and viomycin is located on the ribosomal subunit interface close to nucleotides C1409 in...
MYCOBACTERIUM-TUBERCULOSIS | ANGSTROM RESOLUTION | ANTIBIOTICS | BACTERIAL RIBOSOME | MESSENGER-RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MICROBIOLOGY | POSTTRANSCRIPTIONAL MODIFICATIONS | DRUG-RESISTANCE | THERMUS-THERMOPHILUS | 70S RIBOSOME | tRNA Methyltransferases - metabolism | Bacteria - drug effects | Bacterial Proteins - genetics | Models, Molecular | RNA, Ribosomal - metabolism | Viomycin - pharmacology | Capreomycin - pharmacology | Microbial Sensitivity Tests | tRNA Methyltransferases - genetics | Bacteria - enzymology | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Methylation | Nucleic Acid Conformation | Ribosome Subunits - metabolism | capreomycin | mRNA translation | rRNA | rRNA methyltransferase | ribosomal subunit interface | viomycin | 2′-O-methylation
MYCOBACTERIUM-TUBERCULOSIS | ANGSTROM RESOLUTION | ANTIBIOTICS | BACTERIAL RIBOSOME | MESSENGER-RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MICROBIOLOGY | POSTTRANSCRIPTIONAL MODIFICATIONS | DRUG-RESISTANCE | THERMUS-THERMOPHILUS | 70S RIBOSOME | tRNA Methyltransferases - metabolism | Bacteria - drug effects | Bacterial Proteins - genetics | Models, Molecular | RNA, Ribosomal - metabolism | Viomycin - pharmacology | Capreomycin - pharmacology | Microbial Sensitivity Tests | tRNA Methyltransferases - genetics | Bacteria - enzymology | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Methylation | Nucleic Acid Conformation | Ribosome Subunits - metabolism | capreomycin | mRNA translation | rRNA | rRNA methyltransferase | ribosomal subunit interface | viomycin | 2′-O-methylation
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Loading RightsNucleic Acids Research, ISSN 0305-1048, 2017, Volume 45, Issue 19, pp. 11043 - 11055
In prokaryotes, RNA polymerase and ribosomes can bind concurrently to the same RNA transcript, leading to the functional coupling of transcription and...
LIVE ESCHERICHIA-COLI | MESSENGER-RNA | TERMINAL DOMAIN | ALPHA-SUBUNIT | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | BACTERIAL TRANSCRIPTION | ELONGATION-FACTOR | GTP HYDROLYSIS | 70S RIBOSOME | Ribosome Subunits - chemistry | Protein Biosynthesis | Models, Molecular | Escherichia coli Proteins - metabolism | Escherichia coli - genetics | Escherichia coli - metabolism | Protein Binding | Protein Domains | Transcription, Genetic | DNA-Directed RNA Polymerases - chemistry | Kinetics | Ribosome Subunits - genetics | DNA-Directed RNA Polymerases - metabolism | Escherichia coli Proteins - chemistry | Ribosome Subunits - metabolism | Gene regulation, Chromatin and Epigenetics
LIVE ESCHERICHIA-COLI | MESSENGER-RNA | TERMINAL DOMAIN | ALPHA-SUBUNIT | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | BACTERIAL TRANSCRIPTION | ELONGATION-FACTOR | GTP HYDROLYSIS | 70S RIBOSOME | Ribosome Subunits - chemistry | Protein Biosynthesis | Models, Molecular | Escherichia coli Proteins - metabolism | Escherichia coli - genetics | Escherichia coli - metabolism | Protein Binding | Protein Domains | Transcription, Genetic | DNA-Directed RNA Polymerases - chemistry | Kinetics | Ribosome Subunits - genetics | DNA-Directed RNA Polymerases - metabolism | Escherichia coli Proteins - chemistry | Ribosome Subunits - metabolism | Gene regulation, Chromatin and Epigenetics
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12.
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GTP hydrolysis by EF‐G synchronizes tRNA movement on small and large ribosomal subunits
The EMBO Journal, ISSN 0261-4189, 05/2014, Volume 33, Issue 9, pp. 1073 - 1085
Elongation factor G (EF‐G) promotes the movement of two tRNAs and the mRNA through the ribosome in each cycle of peptide elongation. During translocation, the...
translation | protein synthesis | ribosome | molecular machines | movement | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELONGATION-FACTOR-G | ESCHERICHIA-COLI | TRANSLATION ELONGATION | PROTEIN-SYNTHESIS | 70S RIBOSOME | CELL BIOLOGY | HYBRID-STATE | INTERSUBUNIT ROTATION | INTERMEDIATE STATES | SINGLE RIBOSOMES | PEPTIDYL-TRANSFER-RNA | Protein Biosynthesis | Ribosome Subunits, Small, Bacterial - metabolism | Movement | RNA Transport | Ribosome Subunits, Large, Bacterial - metabolism | Guanosine Triphosphate - metabolism | Hydrolysis | RNA, Transfer - physiology | Escherichia coli - genetics | Escherichia coli - metabolism | Peptide Elongation Factor G - metabolism | Kinetics | Organisms, Genetically Modified | Bacteriology | Ribosomal DNA
translation | protein synthesis | ribosome | molecular machines | movement | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELONGATION-FACTOR-G | ESCHERICHIA-COLI | TRANSLATION ELONGATION | PROTEIN-SYNTHESIS | 70S RIBOSOME | CELL BIOLOGY | HYBRID-STATE | INTERSUBUNIT ROTATION | INTERMEDIATE STATES | SINGLE RIBOSOMES | PEPTIDYL-TRANSFER-RNA | Protein Biosynthesis | Ribosome Subunits, Small, Bacterial - metabolism | Movement | RNA Transport | Ribosome Subunits, Large, Bacterial - metabolism | Guanosine Triphosphate - metabolism | Hydrolysis | RNA, Transfer - physiology | Escherichia coli - genetics | Escherichia coli - metabolism | Peptide Elongation Factor G - metabolism | Kinetics | Organisms, Genetically Modified | Bacteriology | Ribosomal DNA
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