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. 1985 Nov;82(22):7676–7680. doi: 10.1073/pnas.82.22.7676

Primary structure of phage mu transposase: homology to mu repressor.

R M Harshey, E D Getzoff, D L Baldwin, J L Miller, G Chaconas
PMCID: PMC391396  PMID: 2999776

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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