Characterizing protein-nucleic acid interactions with challenge phages

Thomas E. Numrych; Jeffrey F. Gardner

doi:10.1016/S1044-5773(05)80004-6

Characterizing protein-nucleic acid interactions with challenge phages

Thomas E. Numrych, Jeffrey F. Gardner

Microbiology

Research output: Contribution to journal › Article › peer-review

Abstract

Challenge phages are modified versions of bacteriophage P22 that are designed to study protein-nucleic acid interactions in vivo using the phage ant gene as a reporter. ant encodes a regulator of the lysogenic response, and its activity can be easily and sensitively monitored. P22 challenge phages can be used to characterize many different sequence-specific protein-DNA interactions by constructing derivatives that contain DNA binding sites of interest. The foreign DNA binding site is substituted for the phage O_mnt operator, which controls ant transcription. In addition, challenge phages can be constructed to characterize protein-RNA interactions by substituting DNA encoding the appropriate RNA binding site upstream of the translation start of the ant gene. Specific applications of challenge phages will be discussed.

Original language	English (US)
Pages (from-to)	5-13
Number of pages	9
Journal	Seminars in Virology
Volume	6
Issue number	1
DOIs	https://doi.org/10.1016/S1044-5773(05)80004-6
State	Published - Feb 1995

Keywords

DNA-protein interactions
P22 challenge phage
RNA-protein interactions
altered DNA-binding specificity
higher-order complexes

ASJC Scopus subject areas

Immunology
Virology

Online availability

10.1016/S1044-5773(05)80004-6

Library availability

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title = "Characterizing protein-nucleic acid interactions with challenge phages",

abstract = "Challenge phages are modified versions of bacteriophage P22 that are designed to study protein-nucleic acid interactions in vivo using the phage ant gene as a reporter. ant encodes a regulator of the lysogenic response, and its activity can be easily and sensitively monitored. P22 challenge phages can be used to characterize many different sequence-specific protein-DNA interactions by constructing derivatives that contain DNA binding sites of interest. The foreign DNA binding site is substituted for the phage Omnt operator, which controls ant transcription. In addition, challenge phages can be constructed to characterize protein-RNA interactions by substituting DNA encoding the appropriate RNA binding site upstream of the translation start of the ant gene. Specific applications of challenge phages will be discussed.",

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author = "Numrych, {Thomas E.} and Gardner, {Jeffrey F.}",

note = "Funding Information: We thank Laura Hales, Erik Read and Bob Weisberg for constructive comments on the manuscript. Work done in the authors' laboratory was supported by a grant from the National Institutes of Health.",

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AU - Numrych, Thomas E.

AU - Gardner, Jeffrey F.

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N2 - Challenge phages are modified versions of bacteriophage P22 that are designed to study protein-nucleic acid interactions in vivo using the phage ant gene as a reporter. ant encodes a regulator of the lysogenic response, and its activity can be easily and sensitively monitored. P22 challenge phages can be used to characterize many different sequence-specific protein-DNA interactions by constructing derivatives that contain DNA binding sites of interest. The foreign DNA binding site is substituted for the phage Omnt operator, which controls ant transcription. In addition, challenge phages can be constructed to characterize protein-RNA interactions by substituting DNA encoding the appropriate RNA binding site upstream of the translation start of the ant gene. Specific applications of challenge phages will be discussed.

AB - Challenge phages are modified versions of bacteriophage P22 that are designed to study protein-nucleic acid interactions in vivo using the phage ant gene as a reporter. ant encodes a regulator of the lysogenic response, and its activity can be easily and sensitively monitored. P22 challenge phages can be used to characterize many different sequence-specific protein-DNA interactions by constructing derivatives that contain DNA binding sites of interest. The foreign DNA binding site is substituted for the phage Omnt operator, which controls ant transcription. In addition, challenge phages can be constructed to characterize protein-RNA interactions by substituting DNA encoding the appropriate RNA binding site upstream of the translation start of the ant gene. Specific applications of challenge phages will be discussed.

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Characterizing protein-nucleic acid interactions with challenge phages

Abstract

Keywords

ASJC Scopus subject areas

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