DNA sequence requirements for the activation of 434 P(RM) transcription by 434 repressor

DNA and Cell Biology

Volumn 19, Issue 10, 2000, Pages 621-630

  Xu, J ^a   Koudelka, G B ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; REPRESSOR PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE; BINDING SITE; CONFORMATIONAL TRANSITION; DNA SEQUENCE; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN INDUCTION; REPRESSOR GENE; STRUCTURE ANALYSIS; TRANSCRIPTION INITIATION;

AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; BINDING, COMPETITIVE; DIMERIZATION; DNA, VIRAL; DNA-DIRECTED RNA POLYMERASES; GENE EXPRESSION REGULATION, VIRAL; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN SUBUNITS; REPRESSOR PROTEINS; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION, GENETIC; VIRAL PROTEINS;

EID: 0033784681     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/104454900750019380     Document Type: Article

References (30)

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13. Amino acid substitutions in the -35 recognition motif of sigma 70 that result in defects in phage lambda repressor-stimulated transcription
14. Influence of a steroid receptor DNA-binding domain on transcriptional regulatory functions
15. Target of the transcriptional activation function of phage lambda cI protein
16. A general and fast method to generate multiple site directed mutations
17. The two alpha subunits of Escherichia coli RNA polymerase are asymmetrically arranged and contact different halves of the DNA upstream element
18. AraC protein can activate transcription from only one position and when pointed in only one direction
19. The complex between phage 434 repressor DNA-binding domain and operator site OR3: Structural differences between consensus and non-consensus half-sites
20. A third recognition element in bacterial promoters: DNA binding by the a subunit of RNA polymerase
21. Location, structure, and function of the target of a transcriptional activator protein
22. Upstream interactions at the lambda pRM promoter are sequence nonspecific and activate the promoter to a lesser extent than an introduced LIP element of an rRNA promoter
23. Substituting an α-helix switches the sequence specific DNA interactions of a repressor
24. A new-specificity mutant of 434 repressor that defines an amino acid-base pair contact
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28. Mutations changing the specificity on an RNA polymerase sigma factor