2007
DOI: 10.1016/j.jmb.2006.09.088
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Abstract: Assembly of bacteriophage P22 procapsids has long served as a model for assembly of spherical viruses. Historically, assembly of viruses has been treated as a non-equilibrium process. Recently alternative models have been developed that treat spherical virus assembly as an equilibrium process. Here we have investigated whether P22 procapsids assembly reactions achieve equilibrium or are irreversibly trapped. To assemble a procapsid-like particle in vitro, pure coat protein monomers are mixed with scaffolding p… Show more

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Cited by 30 publications
(32 citation statements)
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References 54 publications
(32 reference statements)
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“…While insertion of the final subunit is also slowed by excluded volume constraints for the present model, we find that once completed, capsids are stable and dissociation of a subunit is slow compared to assembly timescales. This result seems consistent with experimental observations that subunit exchange between completed P22 capsids and free subunits is characterized by long timescales (days) compared to those for assembly (minutes) [75,76].…”
Section: A Modeling Empty Capsid Formationsupporting
confidence: 92%
“…While insertion of the final subunit is also slowed by excluded volume constraints for the present model, we find that once completed, capsids are stable and dissociation of a subunit is slow compared to assembly timescales. This result seems consistent with experimental observations that subunit exchange between completed P22 capsids and free subunits is characterized by long timescales (days) compared to those for assembly (minutes) [75,76].…”
Section: A Modeling Empty Capsid Formationsupporting
confidence: 92%
“…22 Experimentally, reversibility can be indicated by exchange with free subunit. 23 The extent of assembly in the irreversible reaction does not show the correct concentration dependence (unlike the case shown in Fig. 1B), but when there are hundreds of subunits per capsid the slope may be experimentally inaccessible.…”
mentioning
confidence: 87%
“…Studies on folding defects of mutant coat proteins (S223F and F353L) have shown that a suppressor of these mutations (T166I) appears to increase the binding of coat protein to scaffolding protein, thereby allowing proper PC assembly (75,76). Moreover, folding defects of the coat protein mutants can be rescued by the presence of the GroE folding chaperone system (77)(78)(79).…”
Section: The Structure Of the Scaffolding Protein C-terminal Hth Ismentioning
confidence: 99%