B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer.
A DNA strand-transfer reaction is an early step in the transposition of phage Mu. It has been shown that an efficient reaction in vitro requires, in addition to buffer and salt, only the Mu A protein, Mu B protein, host protein HU, ATP, and Mg2+. We have determined that, of the three protein factors involved, only the Mu B protein has an ATPase activity. The Mu B ATPase is stimulated by Mu A protein and DNA but not by either of these factors alone. Double-stranded DNA is a much better cofactor than single-stranded DNA, but there is no apparent sequence specificity. In the absence of the Mu B protein and/or ATP, the intermolecular Mu DNA strand-transfer reaction is extremely inefficient, and the strand-transfer products are predominantly the result of an intramolecular reaction. This contrasts with the efficient intermolecular reaction that occurs if Mu B protein and ATP are provided. The Mu B protein, in the presence of Mu A protein and protein HU, therefore, seems to facilitate interactions between potential DNA target sites and pairs of Mu DNA ends.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D003090:Coliphages / Q000201:enzymology*; D004279:DNA, Viral / Q000378:metabolism* / Q000648:ultrastructure; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D014764:Viral Proteins / Q000378:metabolism*
D004279:DNA, Viral; D014764:Viral Proteins; D000251:Adenosine Triphosphatases