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• W2116731188 abstract "ABSTRACT NucC is structurally and functionally homologous to a family of prokaryotic zinc finger transcription factors required for late gene expression in P2- and P4-related bacteriophages. Characterization of these proteins in vitro has been hampered by their relative insolubility and tendency to aggregate. We report here the successful purification of soluble, active, wild-type NucC protein. Purified NucC exhibits site-specific binding to a conserved DNA sequence that is located upstream of NucC-dependent Serratia marcescens promoters and the late promoters of P2-related phages. This sequence is sufficient for binding of NucC in vitro. NucC binding to the S. marcescens nuclease promoter P nucA and to the sequence upstream of the P2 late promoter P F is accompanied by DNA bending. NucC protects about 25 nucleotides of the P F upstream region from DNase I digestion, and RNA polymerase protects the promoter region only in the presence of NucC. Template DNA, RNA polymerase holoenzyme, and purified NucC are the only macromolecular components required for transcription from P F in vitro." @default.
• W2116731188 created "2016-06-24" @default.
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• W2116731188 date "2003-03-15" @default.
• W2116731188 modified "2023-09-24" @default.
• W2116731188 title "Purification and In Vitro Characterization of the Serratia marcescens NucC Protein, a Zinc-Binding Transcription Factor Homologous to P2 Ogr" @default.
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• W2116731188 doi "https://doi.org/10.1128/jb.185.6.1808-1816.2003" @default.
• W2116731188 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/150115" @default.
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