Detail Escherichia coli DNA Topoisomerase I Copurifies withTn5 Transposase, and Tn5 TransposaseInhibits Topoisomerase I Bibliografi Author: Yigit, Hesna ; reznikoff, William S. (Co-Author) Bahasa: (EN )    Edisi: Journal of Bacteriology, Mei 1999     Penerbit: American Society for Microbiology      Jenis: Journal - ilmiah internasional Fulltext: Ecoli Tn5_DNA Topoisomerase I.pdf (2.69MB; 0 download) Abstract Tn5 transposase (Tnp) overproduction is lethal to Escherichia coli. Genetic evidence suggested that this killing involves titration of E. coli topoisomerase I (Topo I). Here, we present biochemical evidence that supports this model. Tn5 Tnp copurifies with Topo I while nonkilling derivatives of Tnp, D37Tnp and D55Tnp (Inhibitor [Inh]), show reduced affinity or no affinity, respectively, for Topo I. In agreement with these results, the presence of Tnp, but not D37 or Inh derivatives of Tnp, inhibits the DNA relaxation activity of Topo I in vivo as well as in vitro. Other proteins, including RNA polymerase, are also found to copurify with Tnp. For RNA polymerase, reduced copurification with Tnp is observed in extracts from a topA mutant strain, suggesting that RNA polymerase interacts with Topo I and not Tnp. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Lihat Sejarah Pengadaan  Konversi Metadata   Kembali

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