Primary structure of phage mu transposase: homology to mu repressor.
The phage Mu transposase is essential for integration, replication-transposition, and excision of Mu DNA. We present the complete nucleotide and derived amino acid sequence of the transposase and analyze implications for transposase/DNA interaction. The NH2 terminus of the Mu transposase has considerable sequence homology with the Mu repressor and with the NH2 terminus of the transposase of the Mu-like phage D108. These three proteins are known to share binding sites on DNA. The protein sequence and predicted secondary structural similarities at the NH2 termini of the three proteins suggest a common DNA-binding region similar to the regions found in proteins of known structure. An internal sequence in the Mu A protein also shares these features. We anticipate that these regions will be involved in DNA recognition during transposition.
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics*; D001483:Base Sequence; D001665:Binding Sites; D004251:DNA Transposable Elements; D004268:DNA-Binding Proteins / Q000032:analysis; D009713:Nucleotidyltransferases / Q000032:analysis*; D012097:Repressor Proteins / Q000032:analysis*; D014157:Transcription Factors / Q000032:analysis*; D019895:Transposases
D004251:DNA Transposable Elements; D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D009713:Nucleotidyltransferases; D019895:Transposases