Journal of Molecular Biology
Control by bacteriophage T4 of two sequential phosphorylations of the alpha subunit of Escherichia coli RNA polymerase☆
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Cited by (34)
Chapter 2 RNA Processing and Decay in Bacteriophage T4
2009, Progress in Molecular Biology and Translational ScienceCitation Excerpt :A well‐known target of this modification is the α‐subunit of the host RNA polymerase. But other as yet unidentified E. coli proteins are ADP‐ribosylated (29–31). Noncovalent modifications, such as the binding of T4 polypeptides to host proteins, include the well‐described alteration of host RNA polymerase by several T4 proteins that lead to a modification of its specificity throughout phage development (10).
Chapter 2 RNA Processing and Decay in Bacteriophage T4
2009, Progress in Nucleic Acid Research and Molecular BiologyCitation Excerpt :A well‐known target of this modification is the α‐subunit of the host RNA polymerase. But other as yet unidentified E. coli proteins are ADP‐ribosylated (29–31). Noncovalent modifications, such as the binding of T4 polypeptides to host proteins, include the well‐described alteration of host RNA polymerase by several T4 proteins that lead to a modification of its specificity throughout phage development (10).
The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: Target proteins identified
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The α-subunit of this enzyme is modified in a two-step process by the T4 enzymes Alt and ModA. First, the 70-kDa gpAlt efficiently ADP-ribosylates one of the two α-subunits of the host RNAP in the carboxy-terminal domain, at position Arg265[3,39,40]. In a second step, ModA targets both α-subunits of the host enzyme, again at residue Arg265[26].
Flow cytometric analysis of CFP-YFP FRET as a marker for in vivo protein-protein interaction
2005, Clinical and Applied Immunology ReviewsCitation Excerpt :Given the significance of protein interactions, it is no surprise that a variety of assays have been developed for their study [5,9,10]. These include long-used biochemical techniques such as affinity chromatography [11] and co-immunoprecipitation [12], widely used genetic screens such as the yeast 2-hybrid system and its derivatives [10,13], and more recently developed biophysical approaches such as surface plasmon resonance [14–16]. This review describes a protein–protein interaction assay that uses a relatively recent application of some relatively old scientific principles: the analysis of fluorescence resonance energy transfer (FRET) between cyan fluorescent protein (CFP) and yellow fluorescent protein (YFP) by flow cytometry.
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This research was supported by National Institutes of Health grant no. GM09541 to Dr W. Gilbert.
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Present address: Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England.