Structure-based analysis of RNA polymerase function: The largest subunit's rudder contributes critically to elongation complex stability and is not involved in the maintenance of RNA-DNA hybrid length

EMBO Journal

Volumn 21, Issue 6, 2002, Pages 1369-1378

  Kuznedelov, Konstantin ^a   Korzheva, Nataliya ^a   Mustaev, Arkady ^a   Severinov, Konstantin ^b  

^a DIVISION OF REPRODUCTIVE BIOLOGY   (United States)

^b RUTGERS UNIVERSITY   (United States)

Author keywords

Localized DNA melting; RNA polymerase; Transcription complex; Transcription complex stability; Transcription termination

Indexed keywords

DNA; MUTANT PROTEIN; RECOMBINANT ENZYME; RECOMBINANT RNA POLYMERASE; RNA; RNA POLYMERASE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DNA DENATURATION; DNA RNA HYBRIDIZATION; DNA STRAND; DNA TEMPLATE; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBUNIT; GENE MUTATION; GENETIC CONSERVATION; MOLECULAR EVOLUTION; MOLECULAR INTERACTION; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STABILITY; RNA TRANSLATION; STRUCTURE ACTIVITY RELATION; THERMUS AQUATICUS; TRANSCRIPTION REGULATION; TRANSCRIPTION TERMINATION;

AMINO ACID SEQUENCE; BASE PAIR MISMATCH; DNA; DNA-DIRECTED RNA POLYMERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; NUCLEIC ACID HYBRIDIZATION; PEPTIDE CHAIN ELONGATION, TRANSLATIONAL; PROMOTER REGIONS (GENETICS); PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RNA; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPLATES, GENETIC; THERMUS; TRANSCRIPTION, GENETIC;

NEGIBACTERIA; THERMUS; THERMUS AQUATICUS;

EID: 0037086450     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/21.6.1369     Document Type: Article

References (19)

1. Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases
2. Recombinant Escherichia coli RNA polymerase: Purification of individually overexpressed subunits and in vitro assembly
3. 70 with core RNA polymerase
4. New models for the mechanism of transcription elongation and its regulation
5. Structural basis of transcription: RNA polymerase II at 2.8 Å resolution
6. Open complex formation by Escherichia coli RNA polymerase: The mechanism of polymerase-induced strand separation of double helical DNA
7. RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II
8. Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
9. Studies on the functional topography of Escherichia coli RNA polymerase. Highly selective affinity labeling by analogues of initiating substrates
10. Transcription elongation complex: Structure and function
11. Mechanistic model of the elongation complex of Escherichia coli RNA polymerase
12. A structural model of transcription elongation
13. Recombinant Thermus aquaticus RNA polymerase - A new tool for structure-based analysis of transcription
14. Structural organization of the RNA polymerase-promoter open complex
15. Dissection of two hallmarks of the open promoter complex by mutation in RNA polymerase core subunit
16. Transcription processivity: Protein-DNA interactions holding together the elongation complex
17. RNA-DNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase
18. A mutant RNA polymerase that forms unusual open promoter complexes
19. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution