Host proteins can stimulate Tn7 transposition: a novel role for the ribosomal protein L29 and the acyl carrier protein.
The bacterial transposon Tn7 is distinguished by its ability to insert at a high frequency into a specific site in the Escherichia coli chromosome called attTn7. Tn7 insertion into attTn7 requires four Tn7-encoded transposition proteins: TnsA, TnsB, TnsC and TnsD. The selection of attTn7 is determined by TnsD, a sequence-specific DNA-binding protein. TnsD binds attTn7 and interacts with TnsABC, the core transposition machinery, which facilitates the insertion of Tn7 into attTn7. In this work, we report the identification of two host proteins, the ribosomal protein L29 and the acyl carrier protein (ACP), which together stimulate the binding of TnsD to attTn7. The combination of L29 and ACP also stimulates Tn7 transposition in vitro. Interestingly, mutations in L29 drastically decrease Tn7 transposition in vivo, and this effect of L29 on Tn7 transposition is specific for TnsABC+D reactions.
The Johns Hopkins University School of Medicine, Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, 725 North Wolfe Street, Room 601 PCTB, Baltimore, MD 21205, USA.
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Sharpe
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Craig
D000213:Acyl Carrier Protein / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D004251:DNA Transposable Elements; D004926:Escherichia coli / Q000235:genetics*; D011995:Recombination, Genetic; D012269:Ribosomal Proteins / Q000378:metabolism*
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; D004251:DNA Transposable Elements; D012269:Ribosomal Proteins; C035078:ribosomal protein L29