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Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus.


ABSTRACT: 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.

SUBMITTER: Scheele U 

PROVIDER: S-EPMC3126172 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus.

Scheele Urte U   Erdmann Susanne S   Ungewickell Ernst J EJ   Felisberto-Rodrigues Catarina C   Ortiz-Lombardía Miguel M   Garrett Roger A RA  

Journal of virology 20110302 10


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 prot  ...[more]

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