Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus
Research output: Contribution to journal › Journal article › Research › peer-review
The crenarchaeal Acidianus two-tailed virus (ATV) undergoes a remarkable morphological development, extracellularly and independently of host cells, by growing long tails at each end of a spindle-shaped virus particle. Initial work suggested that an intermediate filament-like protein, p800, is involved in this process. We propose that an additional chaperone system is required, consisting of a MoxR-type AAA ATPase (p618) and a von Willebrand domain A (VWA)-containing cochaperone, p892. Both proteins are absent from the other known bicaudavirus, STSV1, which develops a single tail intracellularly. p618 exhibits ATPase activity and forms a hexameric ring complex that closely resembles the oligomeric complex of the MoxR-like protein RavA (YieN). ATV proteins p387, p653, p800, and p892 interact with p618, and with the exception of p800, all bind to DNA. A model is proposed to rationalize the interactions observed between the different protein and DNA components and to explain their possible structural and functional roles in extracellular tail development.
Original language | English |
---|---|
Journal | Journal of Virology |
Volume | 85 |
Issue number | 10 |
Pages (from-to) | 4812-4821 |
Number of pages | 10 |
ISSN | 1098-5514 |
DOIs | |
Publication status | Published - 2011 |
ID: 33493676