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1. Full Text Structural Basis for Promoter −10 Element Recognition by the Bacterial RNA Polymerase σ Subunit
by Feklistov, Andrey and Darst, Seth A
Cell, ISSN 0092-8674, 2011, Volume 147, Issue 6, pp. 1257 - 1269
The key step in bacterial promoter opening is recognition of the −10 promoter element (T A T A A T consensus sequence) by the RNA polymerase σ subunit. We... 
Promoter Regions, Genetic | Sigma Factor - chemistry | Sigma Factor - metabolism | DNA, Single-Stranded - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Crystallography, X-Ray | Escherichia coli Proteins - metabolism | DNA, Single-Stranded - chemistry | Base Pairing | Base Sequence | Escherichia coli - metabolism | Hydrophobic and Hydrophilic Interactions | Bacterial Proteins - metabolism | DNA-Directed RNA Polymerases - chemistry | DNA-Directed RNA Polymerases - metabolism | Escherichia coli Proteins - chemistry | Thermus - metabolism | Index Medicus
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2. Full Text Structural insight into cap-snatching and RNA synthesis by influenza polymerase
by Reich, Stefan and Reich, Stefan and Guilligay, Delphine and Pflug, Alexander and Malet, Helene and Berger, Imre and Crepin, Thibaut and Hart, Darren and Lunardi, Thomas and Nanao, Max and Ruigrok, Rob W. H and Cusack, Stephen
Nature, ISSN 0028-0836, 12/2014, Volume 516, Issue 7531, pp. 361 - 366
Influenza virus polymerase uses a capped primer, derived by 'cap-snatching' from host pre-messenger RNA, to transcribe its RNA genome into mRNA and a... 
MESSENGER-RNAS | IN-VITRO | MAXIMUM-LIKELIHOOD | ENDONUCLEASE | REPLICATION | ACTIVE-SITE | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | P-PROTEINS | VIRUS VIRION RNA | SUBUNIT | Protein Structure, Tertiary | Influenza A virus - chemistry | Influenza B virus - enzymology | Promoter Regions, Genetic | Catalytic Domain | RNA, Viral - biosynthesis | Crystallization | Models, Molecular | Influenza A virus - enzymology | RNA Caps - metabolism | RNA, Viral - chemistry | Virus Replication | Gene Expression Regulation, Viral | Protein Binding | RNA Caps - chemistry | Influenza B virus - chemistry | DNA-Directed RNA Polymerases - chemistry | DNA-Directed RNA Polymerases - metabolism | Influenza viruses | Synthesis | RNA | Analysis | Crystals | Research | Structure | Health aspects | RNA polymerases | Ribonucleic acid--RNA | Influenza | Binding sites | Crystal structure | Index Medicus | Biochemistry, Molecular Biology | RNA Caps | Influenza B virus | Life Sciences | DNA-Directed RNA Polymerases | Influenza A virus | RNA, Viral | Biomolecules
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3. Full Text Nucleosomes Are Context-Specific, H2A.Z-Modulated Barriers to RNA Polymerase
by Weber, Christopher M and Ramachandran, Srinivas and Henikoff, Steven
Molecular Cell, ISSN 1097-2765, 03/2014, Volume 53, Issue 5, pp. 819 - 830
Nucleosomes are barriers to transcription in vitro; however, their effects on RNA polymerase in vivo are unknown. Here we describe a simple and general... 
ORGANIZATION | INITIATION | TRANSCRIPT ELONGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENOME-WIDE | HISTONE VARIANTS | GENE-REGULATION | POL II | ACTIVE GENES | H2A.Z | DROSOPHILA | CELL BIOLOGY | Cytoplasm - chemistry | Cell Line | Promoter Regions, Genetic | Phosphorylation | Reproducibility of Results | Histones - chemistry | Nucleosomes - chemistry | Drosophila | RNA - chemistry | Animals | RNA Interference | Transcription, Genetic | DNA-Directed RNA Polymerases - chemistry | Transgenes | RNA Polymerase II - chemistry | Chromatin - chemistry | RNA | Molecular biology | Genetic transcription | Index Medicus
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4. Full Text Structure of influenza A polymerase bound to the viral RNA promoter
by Pflug, Alexander and Pflug, Alexander and Guilligay, Delphine and Reich, Stefan and Cusack, Stephen
Nature, ISSN 0028-0836, 12/2014, Volume 516, Issue 7531, pp. 355 - 360
The influenza virus polymerase transcribes or replicates the segmented RNA genome (viral RNA) into viral messenger RNA or full-length copies. To initiate RNA... 
CAPPED RNAS | HEPATITIS-C VIRUS | MESSENGER-RNA | TERMINAL DOMAIN | VIRUS PB1 PROTEIN | ACTIVE-SITE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MUTATIONAL ANALYSIS | VIRION RNA | ENDONUCLEASE ACTIVITY | Protein Structure, Tertiary | Promoter Regions, Genetic | RNA, Viral - chemistry | Crystallization | Models, Molecular | Protein Binding | DNA-Directed RNA Polymerases - chemistry | Protein Subunits - chemistry | Influenza A virus - enzymology | Binding Sites | Influenza viruses | Physiological aspects | Influenza | RNA polymerases | Genomes | Ribonucleic acid--RNA | Binding sites | Crystal structure | Index Medicus
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5. Full Text A cross-chiral RNA polymerase ribozyme
by Sczepanski, Jonathan T and Joyce, Gerald F
Nature, ISSN 0028-0836, 11/2014, Volume 515, Issue 7527, pp. 440 - 442
Thirty years ago it was shown that the non-enzymatic, template-directed polymerization of activated mononudeotides proceeds readily in a homochiral system, but... 
ACID | MULTIDISCIPLINARY SCIENCES | LIGATION | TEMPLATE | POLYMERIZATION | EXTENSION | MODEL | SELECTION | OLIGONUCLEOTIDES | Biopolymers - chemistry | Oligonucleotides - chemistry | Biocatalysis | Stereoisomerism | RNA, Catalytic - metabolism | Molecular Sequence Data | Polymerization | Templates, Genetic | Directed Molecular Evolution | Origin of Life | RNA - chemistry | Biopolymers - metabolism | RNA - biosynthesis | Oligonucleotides - metabolism | Base Pairing | Base Sequence | Biopolymers - biosynthesis | DNA-Directed RNA Polymerases - chemistry | Evolution, Chemical | Kinetics | DNA-Directed RNA Polymerases - metabolism | Nucleic Acid Conformation | RNA, Catalytic - chemistry | RNA - metabolism | Catalytic RNA | Analysis | RNA polymerases | Enzymes | RNA polymerase | Index Medicus
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6. Full Text Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity
by Sainsbury, Sarah and Martinez-Rucobo, Fuensanta W and Cheung, Alan CM and Cramer, Patrick
The EMBO Journal, ISSN 0261-4189, 04/2011, Volume 30, Issue 7, pp. 1302 - 1310
Related RNA polymerases (RNAPs) carry out cellular gene transcription in all three kingdoms of life. The universal conservation of the transcription machinery... 
RNA polymerase elongation | gene transcription | transcription elongation factor | gene regulation | multiprotein complex structure | INITIATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | COLI NUSG PROTEIN | CELL BIOLOGY | ANGSTROM RESOLUTION | NEGATIVE ELONGATION-FACTOR | IN-VITRO | STRUCTURAL BASIS | SPT5 | THERMUS-THERMOPHILUS | Amino Acid Sequence | Pyrococcus furiosus - chemistry | Repressor Proteins - chemistry | Transcriptional Elongation Factors - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Saccharomyces cerevisiae - chemistry | Sequence Homology, Amino Acid | Protein Structure, Quaternary | Protein Binding | Saccharomyces cerevisiae - enzymology | DNA-Directed RNA Polymerases - chemistry | Chromosomal Proteins, Non-Histone - chemistry | Pyrococcus furiosus - enzymology | Polymerization | Ribonucleic acid--RNA | Genes | Cells | Index Medicus
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7. Full Text Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells
by Bakshi, Somenath and Siryaporn, Albert and Goulian, Mark and Weisshaar, James C
Molecular Microbiology, ISSN 0950-382X, 07/2012, Volume 85, Issue 1, pp. 21 - 38
Quantitative spatial distributions of ribosomes (S2‐YFP) and RNA polymerase (RNAP; β′‐yGFP) in live Escherichia coli are measured by superresolution... 
NUCLEOID-ASSOCIATED PROTEIN | MESSENGER-RNA | BACILLUS-SUBTILIS | CAULOBACTER-CRESCENTUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACTIVE TRANSCRIPTION | B-R | MICROBIOLOGY | BACTERIAL CHROMOSOME SEGREGATION | FLUORESCENT PROTEIN | SPATIAL-DISTRIBUTION | E. COLI | DNA-Directed RNA Polymerases - analysis | Escherichia coli - enzymology | Image Processing, Computer-Assisted | Ribosomes - chemistry | DNA, Bacterial - analysis | DNA-Directed RNA Polymerases - chemistry | Escherichia coli Proteins - chemistry | Escherichia coli Proteins - analysis | Microscopy, Fluorescence | E coli | Microscopy | Microbiology | Fluorescence | RNA polymerase | Ribonucleic acid--RNA | Deoxyribonucleic acid--DNA | Index Medicus
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8. Full Text An atypical RNA polymerase involved in RNA silencing shares small subunits with RNA polymerase II
by Searle, Iain and Jones, Alexandra M E and Vogler, Hannes and Patel, Kanu and Hubner, Nina C and Baulcombe, David C and Huang, Linfeng
Nature Structural & Molecular Biology, ISSN 1545-9993, 01/2009, Volume 16, Issue 1, pp. 91 - 93
Genetic evidence indicates that plant-specific homologs of DNA-dependent RNA polymerase (Pol) II large subunits form Pol IV and Pol V complexes involved in... 
YEAST | BIOPHYSICS | DIRECTED DNA-METHYLATION | RPB7 | FORM | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | ARABIDOPSIS | SIRNA | CELL BIOLOGY | RNA, Small Interfering - genetics | DNA Polymerase beta - chemistry | DNA - metabolism | RNA Polymerase II - metabolism | DNA-Binding Proteins - chemistry | Protein Subunits - metabolism | DNA - genetics | DNA-Binding Proteins - metabolism | Phenotype | RNA Interference | DNA-Directed RNA Polymerases - chemistry | Protein Subunits - chemistry | DNA Polymerase beta - metabolism | DNA-Directed RNA Polymerases - metabolism | DNA Polymerase beta - genetics | RNA Polymerase II - chemistry | RNA, Small Interfering - metabolism | Physiological aspects | Gene silencing | Research | Structure | RNA polymerases | Genetics | RNA polymerase | Molecular biology | Deoxyribonucleic acid--DNA | Botany | Index Medicus
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9. Full Text RNA polymerase pausing and nascent-RNA structure formation are linked through clamp-domain movement
by Hein, Pyae P and Kolb, Kellie E and Windgassen, Tricia and Bellecourt, Michael J and Darst, Seth A and Mooney, Rachel A and Landick, Robert
Nature Structural and Molecular Biology, ISSN 1545-9993, 08/2014, Volume 21, Issue 9, pp. 794 - 802
The rates of RNA synthesis and the folding of nascent RNA into biologically active structures are linked via pausing by RNA polymerase (RNAP). Structures that... 
EXIT CHANNEL | TRIGGER LOOP | INTRINSIC TERMINATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION-TERMINATION | PYRROLO-C | FLAP DOMAIN | CELL BIOLOGY | BIOPHYSICS | IN-VIVO | ALLOSTERIC CONTROL | BETA-SUBUNIT | FACTOR NUSA | RNA Folding | Amino Acid Sequence | Catalytic Domain | Models, Molecular | Molecular Sequence Data | Escherichia coli Proteins - metabolism | Escherichia coli - chemistry | RNA - chemistry | Base Sequence | Escherichia coli - metabolism | Protein Conformation | DNA-Directed RNA Polymerases - chemistry | DNA-Directed RNA Polymerases - metabolism | Escherichia coli Proteins - chemistry | Nucleic Acid Conformation | RNA - metabolism | Synthesis | RNA | Physiological aspects | Genetic research | Research | Structure | RNA polymerases | E coli | Molecular biology | RNA polymerase | Index Medicus
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10. Full Text Structure of human mitochondrial RNA polymerase
by Ringel, Rieke and Sologub, Marina and Morozov, Yaroslav I and Litonin, Dmitry and Cramer, Patrick and Temiakov, Dmitry
Nature, ISSN 0028-0836, 10/2011, Volume 478, Issue 7368, pp. 269 - 273
Transcription of the mitochondrial genome is performed by a single-subunit RNA polymerase (mtRNAP) that is distantly related to the RNAP of bacteriophage T7,... 
TRANSITION | YEAST MITOCHONDRIAL | COMPLEX | SPECIFICITY | TRANSCRIPTION FACTOR-A | PROMOTER RECOGNITION | INITIATION | CRYSTAL-STRUCTURE | ELONGATION | MULTIDISCIPLINARY SCIENCES | TRANSLATION | Protein Structure, Tertiary | Amino Acid Sequence | Mitochondria - enzymology | Nucleic Acid Denaturation | Catalytic Domain | Biocatalysis | Viral Proteins - chemistry | Humans | Models, Molecular | Molecular Sequence Data | Templates, Genetic | Crystallography, X-Ray | DNA - metabolism | Promoter Regions, Genetic - genetics | DNA - genetics | DNA - chemistry | Sequence Alignment | Bacteriophage T7 - enzymology | AT Rich Sequence - genetics | Hydrophobic and Hydrophilic Interactions | DNA-Directed RNA Polymerases - chemistry | DNA-Directed RNA Polymerases - metabolism | Proteins | Enzymes | Biochemistry | Deoxyribonucleic acid--DNA | Fingers & toes | Index Medicus
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11. Full Text Structural basis for transcription elongation by bacterial RNA polymerase
by Artsimovitch, Irina and Vassylyev, Dmitry G and Vassylyeva, Marina N and Perederina, Anna and Tahirov, Tahir H
Nature, ISSN 0028-0836, 07/2007, Volume 448, Issue 7150, pp. 157 - 162
The RNA polymerase elongation complex (EC) is both highly stable and processive, rapidly extending RNA chains for thousands of nucleotides. Understanding the... 
TRANSLOCATION | COMPLEX | MECHANISM | INITIATION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | DNA HYBRID | ELECTRON-DENSITY MAPS | LID ELEMENT | 3.3 ANGSTROM RESOLUTION | THERMUS-THERMOPHILUS | Promoter Regions, Genetic | Thermus thermophilus - enzymology | Thermus thermophilus - chemistry | DNA, Bacterial - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Thermus thermophilus - metabolism | Crystallography, X-Ray | DNA, Bacterial - chemistry | Multiprotein Complexes - metabolism | Thermus thermophilus - genetics | Multiprotein Complexes - chemistry | RNA, Bacterial - chemistry | Bacterial Proteins - metabolism | Transcription, Genetic | DNA-Directed RNA Polymerases - chemistry | DNA-Directed RNA Polymerases - metabolism | Nucleic Acid Conformation | Binding Sites | RNA, Bacterial - metabolism | DNA binding proteins | Research | Genetic transcription | Gene expression | RNA polymerases | Crystallization | Genetics | RNA polymerase | Deoxyribonucleic acid | DNA | Substrates | Binding sites | Polymerase | Ribonucleic acids | Strands | Bacteria | Nucleotides | Elongation | Displacement | Index Medicus
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