Bacteriophage Ø29 protein p6: an architectural protein involved in genome organization, replication and control of transcription

Journal of Molecular Recognition : JMR
Víctor González-HuiciJosé M Hermoso

Abstract

Protein p6 of B. subtilis bacteriophage Ø29 binds to DNA forming a nucleoprotein complex in which the DNA wraps a protein core forming a right-handed superhelix, therefore restraining positive supercoiling and compacting the DNA. The protein does not specifically recognize a nucleotide sequence but rather a structural feature and it binds as a dimer through the minor groove. Protein p6 is in a monomer-dimer equilibrium that shifts to higher-order structures at a concentration of about 1 mM. These structures are probably present in vivo as the intracellular concentration of p6 is estimated to be in this range, and in fact the effective concentration should be still higher due to the macromolecular crowding. The p6 oligomers show an elongated shape compatible with a helical structure reminiscent of the superhelical DNA of the nucleoprotein complex, therefore it was proposed that protein p6 forms a scaffold on which the DNA folds. Since protein p6 is very abundant in infected cells, enough to bind the entire viral progeny, it was proposed to have an architectural role organizing and compacting the viral genome. It has been demonstrated that protein p6 binds in vivo to most, if not all, the Ø29 genome, although with different affin...Continue Reading

Citations

May 2, 2006·Proceedings of the National Academy of Sciences of the United States of America·Bastiano SannaJeffery D Molkentin
Jan 20, 2010·PLoS Pathogens·Charalampos ValmasElke Mühlberger
Jan 1, 2010·International Journal of Molecular Sciences·Ana Camacho, Margarita Salas
Mar 7, 2006·Gene·Víctor González-HuiciJosé M Hermoso
Apr 24, 2010·FEMS Microbiology Reviews·Ana Camacho, Margarita Salas
Aug 23, 2016·Frontiers in Molecular Biosciences·Margarita SalasMiguel de Vega
May 16, 2020·Chembiochem : a European Journal of Chemical Biology·Eszter CsibraVitor B Pinheiro

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