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Gene Review:

phi-8Lp4 - P4

Pseudomonas phage phi8

Juuti, J.T. et al., Paatero, A.O. et al., Ojala, P.M. et al.

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Disease relevance of phi-8Lp4

Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage phi 6 [1].

High impact information on phi-8Lp4

Ca2+ and Zn2+ and non-specific single-stranded RNA stimulate the NTPase activity, while Mg2+ acts as a non-competitive inhibitor, presumably via a separate Mg2+ binding site [1].
The nucleotide specificity and enzymatic properties of the P4 NTPase are similar to the NTP hydrolysis reaction conditions needed to translocate and condense the viral positive-sense RNAs to the procapsid particle [2].
This NTP-binding site is probably different from that of the unspecific viral NTPase found in protein P4 and also from that of the rNTP-specific RNA polymerase active site [3].

References

Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage phi 6. Juuti, J.T., Bamford, D.H., Tuma, R., Thomas, G.J. J. Mol. Biol. (1998) [Pubmed]
Double-stranded RNA bacteriophage phi 6 protein P4 is an unspecific nucleoside triphosphatase activated by calcium ions. Paatero, A.O., Syväoja, J.E., Bamford, D.H. J. Virol. (1995) [Pubmed]
In vitro transcription of the double-stranded RNA bacteriophage phi 6 is influenced by purine NTPs and calcium. Ojala, P.M., Bamford, D.H. Virology (1995) [Pubmed]

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