title: The carboxy-terminal 14 amino acids of phage lambda N protein are dispensable for transcription antitermination.
abstract: The analogous N proteins encoded by lambdoid bacteriophages lambda, 21, and 22 are very different in amino acid sequence, except at their carboxy-terminal ends. Since N lambda remains functional despite the deletion of most of its terminal region of homology to N21, that region of homology cannot represent a region of conserved function.
authors.affiliation: Biology Department, University of Utah, Salt Lake City 84112.
authors.forename: N C
authors.initials: NC
authors.lastname: Franklin
mesh_terms: D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000235:genetics*; D001483:Base Sequence; D002213:Capsid / Q000235:genetics*; D004279:DNA, Viral; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013728:Terminator Regions, Genetic; D014158:Transcription, Genetic; D014758:Viral Core Proteins / Q000235:genetics*
chemical_list: D004279:DNA, Viral; D014758:Viral Core Proteins