The Gam protein of bacteriophage Mu is an orthologue of eukaryotic Ku

d'Adda di Fagagna, Fabrizio, Weller, Geoffrey R, Doherty, Aidan and Jackson, Stephen P (2003) The Gam protein of bacteriophage Mu is an orthologue of eukaryotic Ku. EMBO Reports, 4 (1). pp. 47-52. ISSN 1469-221X

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Abstract

Mu bacteriophage inserts its DNA into the genome of host bacteria and is used as a model for DNA transposition events in other systems. The eukaryotic Ku protein has key roles in DNA repair and in certain transposition events. Here we show that the Gam protein of phage Mu is conserved in bacteria, has sequence homology with both subunits of Ku, and has the potential to adopt a similar architecture to the core DNA-binding region of Ku. Through biochemical studies, we demonstrate that Gam and the related protein of Haemophilus influenzae display DNA binding characteristics remarkably similar to those of human Ku. In addition, we show that Gam can interfere with Ty1 retrotransposition in Saccharomyces cerevisiae. These data reveal structural and functional parallels between bacteriophage Gam and eukaryotic Ku and suggest that their functions have been evolutionarily conserved.

Item Type: Article
Keywords: Amino Acid Sequence Antigens, Nuclear/ chemistry Bacterial Proteins/chemistry Bacteriophage mu/ chemistry/genetics Binding Sites Comparative Study DNA/metabolism DNA Helicases DNA-Binding Proteins/ chemistry Dimerization Eukaryotic Cells/metabolism Evolution, Molecular Haemophilus influenzae/chemistry/genetics Humans Molecular Sequence Data Phylogeny Protein Binding Protein Conformation Protein Structure, Tertiary Research Support, Non-U.S. Gov't Retroelements/genetics Saccharomyces cerevisiae/genetics Sequence Alignment Sequence Homology, Amino Acid Species Specificity Viral Proteins/ chemistry
Schools and Departments: School of Life Sciences > Biochemistry
Research Centres and Groups: Genome Damage and Stability Centre
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Depositing User: Aidan Doherty
Date Deposited: 27 Nov 2006
Last Modified: 24 May 2018 15:55
URI: http://sro.sussex.ac.uk/id/eprint/577
Google Scholar:24 Citations
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