2007
DOI: 10.1379/csc-219r.1
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Abstract: Phage P22 wild-type (WT) coat protein does not require GroEL/S to fold but temperature-sensitive-folding (tsf ) coat proteins need the chaperone complex for correct folding. WT coat protein and all variants absolutely require P22 scaffolding protein, an assembly chaperone, to assemble into precursor structures termed procapsids. Previously, we showed that a global suppressor (su) substitution, T166I, which rescues several tsf coat protein variants, functioned by inducing GroEL/S. This led to an increased forma… Show more

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Cited by 6 publications
(7 citation statements)
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References 62 publications
(78 reference statements)
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“…Likewise, P22 scaffolding protein has been shown to exhibit chaperone-like activity for coat protein variants that have folding defects. Two global suppressors ( su , D163G and T166I) of temperature-sensitive-folding ( tsf ) mutations in P22 coat protein rescue folding via enhanced interaction with scaffolding protein (Parent et al, 2004; Parent and Teschke, 2007). Thus, both HK97’s Δ-domain and P22’s scaffolding protein act as folding chaperones of their coat proteins by promoting assembly to a more stable state by partitioning the precursors to assembled particles before aggregation can occur.…”
Section: Assembly Chaperoned By a Scaffolding Proteinmentioning
confidence: 99%
“…Likewise, P22 scaffolding protein has been shown to exhibit chaperone-like activity for coat protein variants that have folding defects. Two global suppressors ( su , D163G and T166I) of temperature-sensitive-folding ( tsf ) mutations in P22 coat protein rescue folding via enhanced interaction with scaffolding protein (Parent et al, 2004; Parent and Teschke, 2007). Thus, both HK97’s Δ-domain and P22’s scaffolding protein act as folding chaperones of their coat proteins by promoting assembly to a more stable state by partitioning the precursors to assembled particles before aggregation can occur.…”
Section: Assembly Chaperoned By a Scaffolding Proteinmentioning
confidence: 99%
“…Three global su substitutions (D163G, T166I, F170L) were repeatedly and independently isolated from different gene 5 tsf parents, scattered throughout the gene. The tsf:su coat proteins demonstrate both stabilized native and intermediate states as compared to their tsf parents, so that these proteins remain GroEL substrates even though their folding is less defective (Doyle et al, 2004; Parent and Teschke, 2007). The three global su substitutions are located in the β-hinge, which implicates this region as important for folding (Figure 4d).…”
Section: “Let the Phage Do The Work”mentioning
confidence: 99%
“…For example, T166I and D163G both fix the original tsf defects by a shared mechanism. However, F170L corrects tsf protein folding defects by a second mechanism (Aramli and Teschke, 2001; Doyle et al, 2004; Parent and Teschke, 2007). …”
Section: Coat Protein Foldingmentioning
confidence: 99%
See 1 more Smart Citation
“…Although WT coat protein does not require chaperonins to fold in vivo, temperature-sensitive-folding coat mutants can be rescued by overexpression of the GroES/L proteins resulting in viable progeny phage (33)(34)(35). If the E5A and D14A coat mutants cause a folding defect, coexpression of these mutants with extra GroES/L might rescue the assembly of infectious phages, and plating efficiencies would be expected to be similar to that of WT phage.…”
Section: Resultsmentioning
confidence: 99%