Phosphorylation of the integrase protein of coliphage HK022

Mikhail Kolot, Rena Gorovits, Nava Silberstein, Boris Fichtman, Ezra Yagil

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


The integrase (Int) proteins of coliphages HK022 and λ, are phosphorylated in one or more of their tyrosine residues. In Int of HK022 the phosphorylated residue(s) belong to its core-binding/catalytic domains. Wzc, a protein tyrosine kinase of Escherichia coli, is not required for Int phosphorylation in vivo, however, it can transphosphorylate the conserved Tyr342 catalytic residue of Int in vitro. Int purified from cells that overexpress Wzc has a reduced activity in vitro. In vivo, the lysogenization of wild type HK022 as well as of λ is not affected by the overexpression of Wzc. However, the nin5 mutant of λ, which lacks a protein-tyrosine phosphatase gene, shows a significantly reduced lysogenization. It is suggested that phosphorylation of Int by Wzc down regulates the activity of Int.

Original languageEnglish
Pages (from-to)383-390
Number of pages8
Issue number2
StatePublished - 5 Jun 2008
Externally publishedYes


Ilan Rosenshine provided useful advice and strains. Bob Weisberg sent us strains and helped to improve the manuscript. The work was supported by grant number 2003394 from the U.S.–Israel Binational Science Foundation.

FundersFunder number
United States-Israel Binational Science Foundation


    • Integrase
    • Phage HK022
    • Protein phosphorylation
    • Wzc/Wzb


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