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Bacteriophage lambda site-specific recombination.
Van Duyne, Gregory D; Landy, Arthur.
Affiliation
  • Van Duyne GD; Department of Biochemistry & Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
  • Landy A; Department of Molecular Biology, Cell Biology, and Biochemistry, Warren Alpert Medical School, Brown University, Providence, Rhode Island, USA.
Mol Microbiol ; 121(5): 895-911, 2024 05.
Article in En | MEDLINE | ID: mdl-38372210
ABSTRACT
The site-specific recombination pathway of bacteriophage λ encompasses isoenergetic but highly directional and tightly regulated integrative and excisive reactions that integrate and excise the vial chromosome into and out of the bacterial chromosome. The reactions require 240 bp of phage DNA and 21 bp of bacterial DNA comprising 16 protein binding sites that are differentially used in each pathway by the phage-encoded Int and Xis proteins and the host-encoded integration host factor and factor for inversion stimulation proteins. Structures of higher-order protein-DNA complexes of the four-way Holliday junction recombination intermediates provided clarifying insights into the mechanisms, directionality, and regulation of these two pathways, which are tightly linked to the physiology of the bacterial host cell. Here we review our current understanding of the mechanisms responsible for regulating and executing λ site-specific recombination, with an emphasis on key studies completed over the last decade.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Recombination, Genetic / Bacteriophage lambda Language: En Journal: Mol Microbiol Journal subject: BIOLOGIA MOLECULAR / MICROBIOLOGIA Year: 2024 Type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Recombination, Genetic / Bacteriophage lambda Language: En Journal: Mol Microbiol Journal subject: BIOLOGIA MOLECULAR / MICROBIOLOGIA Year: 2024 Type: Article Affiliation country: United States