The α subunit of E. coli RNA polymerase activates RNA binding by NusA

Genes and Development

Volumn 14, Issue 20, 2000, Pages 2664-2675

  Mah, Thien Fah ^a   Kuznedelov, Konstantin ^b   Mushegian, Arcady ^b,c   Severinov, Konstantin ^b   Greenblatt, Jack ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b RUTGERS UNIVERSITY   (United States)

^c Akkadix Corporation   (United States)

Author keywords

subunit; Antitermination; HhH motifs; NusA; RNA binding; Termination

Indexed keywords

BACTERIAL PROTEIN; NUSA PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

ALPHA CHAIN; AMINO ACID SEQUENCE; ARTICLE; BACTERIOPHAGE; CROSS LINKING; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE DELETION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN RNA BINDING; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DNA-DIRECTED RNA POLYMERASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE ELONGATION FACTORS; RNA, BACTERIAL; RNA-BINDING PROTEINS; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

BACTERIA (MICROORGANISMS); BACTERIOPHAGE LAMBDA; ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 0034667947     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.822900     Document Type: Article

References (55)

1. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
2. Conserved domains in DNA repair proteins and evolution of repair systems
3. Interaction of a nascent RNA structure with RNA polymerase is required for hairpin-dependent transcriptional pausing but not for transcript release
4. Domain organization of RNA polymerase α subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding
5. A procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving Polymin P precipitation and DNA-cellulose chromatography
6. The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
7. Transcription antitermination in vitro by λ N gene product: Requirement for a phage nut site and the products of host nusA, nusB, and nusE genes
8. Specificity of the bacteriophage λ N gene product (pN): Nut sequences are necessary and sufficient for antitermination by pN
9. Characterisation of the nucleic-acid-binding activity of KH domains. Different properties of different domains
10. Vigilin, a ubiquitous protein with 14 K homology domains, is the estrogen-inducible vitellogenin mRNA 3'-untranslated region-binding protein
11. The helixhairpin-helix DNA-binding motif: A structural basis for I non-sequence-specific recognition of DNA
12. 70 exhibit specificity of binding to promoter DNA
13. Aminoterminal amino acids modulate σ-factor DNA-binding activity
14. The Escherichia coli RNA polymerase α subunit: Structure and function
15. A bacterial mutant affecting λ development
16. Regulation of phage gene expression by termination and antitermination of transcription
17. Genetic characterization of a bacterial locus involved in the activity of the N function of phage λ
18. Evidence that a nucleotide sequence, 'boxA,' is involved in the action of the NusA protein
19. KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolism
20. The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid
21. The phage λ Q gene product: Activity of a transcription antiterminator in vitro
22. The nusA gene protein of Escherichia coli. Its identification and a demonstration that it interacts with the gene N transcription anti-termination protein of bacteriophage λ
23. Interaction of the σ factor and the nusA gene protein of E. coli with RNA polymerase in the initiation-termination cycle of transcription
24. Termination of transcription by nusA gene protein of Escherichia coli
25. Transcriptional antitermination
26. DNA bending and a flip-out mechanism for base excision by the helixhairpin-helix DNA glycosylase, Escherichia coli AlkA
27. An elongation control particle containing the N gene transcriptional antitermination protein of bacteriophage λ
28. Functional map of the α subunit of Escherichia coli RNA polymerase. Deletion analysis of the amino-terminal assembly domain
29. Isolation and structural analysis of the Escherichia coli trp leader paused transcription complex
30. Crystal structure of NAD(+)-dependent DNA ligase: Modular architecture and functional implications
31. NMR structure of the bacteriophage λ N peptide/boxB RNA complex: Recognition of a GNRA fold by an arginine-rich motif
32. NusA contacts nascent RNA in Escherichia coli transcription complexes
33. Role of Escherichia coli RNA polymerase α subunit in modulation of pausing, termination and anti-termination by the transcription elongation factor NusA
34. Functional importance of regions of Escherichia coli elongation factor NusA that interact with RNA polymerase, the bacteriophage λ N protein and RNA
35. 70 subunit fragment from E. coli RNA polymerase
36. Host factor requirements for processive antitermination of transcription and suppression of pausing by the N protein of bacteriophage λ
37. A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the λ N protein
38. Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage λ N protein
39. Coupling between transcription termination and RNA polymerase inchworming
40. Analysis of nutR: A region of phage λ required for antitermination of transcription
41. The nusA recognition site. Alteration in its sequence or position relative to upstream translation interferes with the action of the N antitermination function of phage λ
42. Control of RNA chain elongation and termination
43. High-affinity RNA ligands to Escherichia coli ribosomes and ribosomal protein S1: Comparison of natural and unnatural binding sites
44. A third recognition element in bacterial promoters: DNA binding by the α subunit of RNA polymerase
45. -: A unique class of mutants defective in the site of gene N product utilization for antitermination of leftward transcription
46. The α subunit of RNA polymerase and transcription termination
47. NusA protein of Escherichia coli is an efficient transcription termination factor for certain terminator sites
48. A workbench for multiple alignment construction and analysis
49. SMART: A web-based tool for the study of genetically mobile domains
50. The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
51. Structure and functions of ribosomal protein S1
52. Rapid RNA polymerase genetics: One-day, no-column preparation of reconstituted recombinant Escherichia coli RNA polymerase
53. nusA amber mutation that causes temperature-sensitive growth of Escherichia coli
54. NusA protein is necessary and sufficient in vitro for phage λ N gene product to suppress a p-independent terminator placed downstream of nutL
55. Reduced p-dependent transcription termination permits NusA-independent growth of Escherichia coli