title: "N" transcription antitermination proteins of bacteriophages lambda, phi 21 and P22.
abstract: Comparison is made among the amino acid sequences of three transcription antitermination proteins, based upon the DNA sequences of their genes in bacteriophages lambda, phi 21 and P22. The three proteins are all small (about 100 amino acids), hydrophilic and basic, but otherwise show little homology. A basic region near the amino terminus has several amino acid positions common to all three proteins and is the locus of mutations that alter six different amino acid positions inactivating the lambda N protein. A less basic region near the center is the locus of three mutations affecting the interaction of lambda N with host nusA protein. The N gene of phi 21 has an amino terminus more like that of P22, and a carboxy terminus clearly related to that of lambda.
authors.forename: N C
authors.initials: NC
authors.lastname: Franklin
mesh_terms: D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000235:genetics; D001483:Base Sequence; D003062:Codon; D003090:Coliphages / Q000235:genetics*; D004279:DNA, Viral; D014176:Protein Biosynthesis; D012483:Salmonella Phages / Q000235:genetics*; D014158:Transcription, Genetic; D014764:Viral Proteins
chemical_list: D003062:Codon; D004279:DNA, Viral; D014764:Viral Proteins