A frameshift mutation at the junction of an IS1 insertion within lacZ restores β-galactosidase activity via formation of an active lacZ-IS1 fusion protein

Michael H. Malamy, Peter T. Rahaim, Charles S. Hoffman, Dwight Baghdoyan, Michael B. O'Connor, Jeff F. Miller

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The insertion of IS1 elements into lacZ results in the loss of β-galactosidase activity, and such insertions exert a severe polar effect on the expression of the distal genes of the operon. In addition to these properties, the mutation lacZ::IS1-MS319 has the unique property of reversion to Lac+ (ts) spontaneously or after treatment with the frameshift mutagen ICR-191; such revertants retain the IS1 element. We have determined that the site of integration of IS1 into lacZ is at position 4338, 18 nucleotides from the end of the sequence encoding the C-terminus of β-galactosidase. Reversion to Lac+ promoted by ICR-191 results from the loss of a G residue from a GGG sequence located at the junction of lacZ and IS1. As a result an active, but temperature-sensitive, lacZ-IS1 fusion protein is formed containing six amino acids derived from IS1 which replace six amino acids encoded by lacZ. The IS1 element in MS319 is a new member of the iso-IS1 family, which we designate IS1T.

Original languageEnglish (US)
Pages (from-to)551-555
Number of pages5
JournalJournal of Molecular Biology
Volume181
Issue number4
DOIs
StatePublished - Feb 20 1985

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