Abstract
The two structural domains of p529, a predicted AAA ATPase of Acidianus two-tailed virus (ATV), were expressed and purified. The N-terminal domain was demonstrated by loss-of-function mutations to carry ATPase activity with a temperature optimum of 60°C. This domain also showed DNA binding activity that was stronger for the whole protein and was weakened in the presence of ATP. The C-terminal domain exhibits Mg 2+-dependent endonuclease activity that was eliminated by site-directed mutagenesis at a conserved catalytic PD. .D/ExK motif. p529 pull-down experiments with cell extracts of Sulfolobus solfataricus demonstrated a specific interaction with Sso1273, corresponding to OppA Ss, an N-linked glycoprotein that specifically binds oligopeptides. The sso1273 gene lies in an operon encoding an oligopeptide/dipeptide ABC transporter system. It is proposed that p529 is involved in ATV-host cell receptor recognition and possibly the endonuclease activity is required for cleavage of the circular viral DNA prior to cell entry.
Original language | English |
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Journal | Virology |
Volume | 421 |
Issue number | 1 |
Pages (from-to) | 61-66 |
Number of pages | 6 |
ISSN | 0042-6822 |
DOIs | |
Publication status | Published - 5 Dec 2011 |