Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus
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Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus. / Scheele, Urte; Erdmann, Susanne; Ungewickell, Ernst J.; Felisberto-Rodrigues, Catarina; Ortiz-Lombardía, Miguel; Garrett, Roger Antony.
I: Journal of Virology, Bind 85, Nr. 10, 2011, s. 4812-4821.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus
AU - Scheele, Urte
AU - Erdmann, Susanne
AU - Ungewickell, Ernst J.
AU - Felisberto-Rodrigues, Catarina
AU - Ortiz-Lombardía, Miguel
AU - Garrett, Roger Antony
PY - 2011
Y1 - 2011
N2 - 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.
AB - 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.
U2 - 10.1128/JVI.00072-11
DO - 10.1128/JVI.00072-11
M3 - Journal article
C2 - 21367903
VL - 85
SP - 4812
EP - 4821
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 10
ER -
ID: 33493676