Abstract
The P22 tailspike protein is a well-studied model system for understanding multimeric protein folding and aggregation. It is one of the few systems for which both in vivo and in vitro folding pathways have been well characterized. Aggregation of the P22 tailspike occurs through a multimeric addition pathway in which both monomeric and multimeric protein can associate with existing aggregates promoting aggregate growth.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
A. Matagne and C. M. Dobson, The folding process of hen lysozyme: a perspective from the “new view,” Cell Mol. Life Sci. 54, 363–371 (1998).
V. Daggett and A. Fersht, The present view of the mechanism of protein folding, Nat. Rev. Mol. Cell Biol. 4, 497–502 (2003).
F. Chiti, E. De Lorenzi, S. Grossi, P. Mangione, S. Giorgetti, G. Caccialanza, C. M. Dobson, G. Merlini, G. Ramponi, and V. Bellotti, A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis, J. Biol. Chem. 276, 46714–46721 (2001).
D. P. Goldenberg and J. King, Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C, J. Mol. Biol. 145, 633–651 (1981).
J. M. Sturtevant, M.-H. Yu, C. Haase-Pettingell, and J. King, Thermostability of temperature-sensitive folding mutants of the P22 tailspike protein. J. Biol. Chem. 264, 10693–10698 (1989).
S. Steinbacher, R. Seckler, S. Miller, B. Steipe, R. Huber, and P. Reinemer, Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer, Science 265, 383–385 (1994).
S. Steinbacher, S. Miller, U. Baxa, N. Budisa, A. Weintraub, R. Seckler, and R. Huber, Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage, J. Mol. Biol. 267, 865–880 (1997).
B. L. Chen and J. King, J. Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase, Biochemistry 30, 6260–6269 (1991).
M. Danner, A. Fuchs, S. Miller, and R. Seckler, Folding and assembly of phage P22 tailspike protein lacking N-terminal, head-binding domain, Eur. J. Biochem. 215, 653–661 (1993).
D. Goldenberg and J. King, Trimeric intermediate in the in vivo folding and subunit assembly of the tailspike endorhamnosidase of bacteriophage P22, Proc. Natl. Acad. Sci. USA 79, 3403–3407 (1982).
D. Goldenberg, D. H. Smith, and J. King, Genetic analysis of the folding pathway for the tailspike protein of phage P22, Proc. Natl. Acad. Sci. USA 80, 7060–7064 (1983).
C. Haase-Pettingell and J. King, Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation a model for inclusion body formation, J. Biol. Chem. 263, 4977–4983 (1988).
J. King and M.-H. Yu, Mutational analysis of protein folding pathways: The P22 tailspike endorhamnosidase, Meth. Enzymol. 131, 250–266 (1986).
M. Danner and R. Seckler, Mechanism of phage P22 tailspike folding mutations, Prot. Sci. 2, 1869–1881 (1993).
M. Beibinger, S. C. Lee, S. Steinbacher, P. Reinemer, R. Huber, M.-H. Yu, and R. Seckler, Mutations that stabilize folding intermediates of phage P22 tailspike protein: Folding in vivo and in vitro, stability, and structural context, J. Mol. Biol. 249, 185–194 (1995).
R. Seckler, A. Fuchs, J. King, and R. Jaenicke, Reconstitution of the thermostable trimeric phage P22 tailspike from denatured chains in vitro, J. Biol. Chem. 264, 11750–11753 (1989).
M. Gage and A. S. Robinson, C-Terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer, Protein Sci. 12, 2732–2747 (2003).
A. S. Robinson and J. King, Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein, Nature Struct. Biol. 4, 450–455 (1997).
C. Haase-Pettingell, S. D. Betts, S. W. Raso, L. Stuart, A. Robinson, and J. King, Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike, Prot. Sci. 10, 397–410 (2000)
B. L. Danek and A. S. Robinson, Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein, Biophys. J. 85, 3237–3247 (2003).
D. Sargent, J. M. Benevides, M.-H. Yu, J. King, and G. J. Thomas, Jr., Secondary structure and thermostability of the phage P22 tailspike. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant, J. Mol. Biol. 199, 491–502 (1988).
M. A. Speed, T. Morshead, D. I. C. Wang, and J. King, Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies, Prot. Sci. 6, 99–108 (1997).
S. D. Betts and J. King, Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation, Prot. Sci. 7, 1516–1523 (1998).
B. G. Lefebvre and A. S. Robinson, Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates, Biotechnol. Bioeng. 82, 595–604 (2003).
D. H. Smith and J. King, Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tailspike protein. III. Intensive polypeptide chains synthesized at 39 degrees C, J. Mol. Biol. 145, 653–676 (1981).
B. Fane and J. King, Identification of sites influencing the folding and subunit assembly of the P22 tailspike polypeptide chain using nonsense mutations, Genetics, 157–171 (1987).
C. Haase-Pettingell and J. King, Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase, J. Mol. Biol. 267, 88–102 (1997).
B. Schuler, F. Furst, F. Osterroth, S. Steinbacher, R. Huber, and R. Seckler, Plasticity and steric strain in a parallel β-helix: rational mutations in the P22 tailspike protein, Proteins: Struct, Funct, Genet. 39, 89–101 (2000).
R. Villafane, A. Fleming, and C. Haase-Pettingell, Isolation of suppressors of temperature-sensitive folding mutations, J. Bacteriol. 176, 137–142 (1994).
B. Fane and J. King, Intragenic suppressors of folding defects in the P22 tailspike protein, Genetics 127, 263–277 (1991).
B. Fane, R. Villafane, A. Mitraki, and J. King, Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein, J. Biol. Chem. 266, 11640–11648 (1991).
B. Schuler and R. Seckler, P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated β-helix domain, J. Mol. Biol. 281, 227–234 (1998).
J. F. Kreisberg, S. D. Betts, C. Haase-Pettingell, and J. King, The interdigitated β-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization, Prot. Sci. 11, 820–830 (2002).
K. Whitehead, The Effects of Chemical Additives on the in vitro Refolding of the P22 Tailspike Protein, Undergraduate Senior Thesis, University of Delaware (2002).
M. Speed, D. I. C. Wang, and J. King, Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tail spike polypeptide chains, Prot. Sci. 4, 900–908 (1995).
B. Friguet, l. Djavadi-Ohaniance, C. Haase-Pettingell, J. King, and M. E. Goldberg, Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase, J. Biol. Chem. 265, 10347–10351 (1990).
M. Speed, Characterization of the Aggregation Pathway Competing with Productive Protein Folding. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, MA (1996).
B. G. Lefebvre, M. J. Gage, and A. S. Robinson, Maximizing recovery of native protein from aggregates by optimizing pressure treatment, Biotechnol. Progr. 20, 623–629 (2004).
B. G. Lefebvre, N. K. Comolli, M. J. Gage, and A. S. Robinson, Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike, Prot. Sci. 13, 1538–15346 (2004).
J. D. Harper, S. S. Wong, C. Lieber, and P. T. Lansbury, Jr., Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease, Biochemistry 38, 8972–8980 (1999).
K. A. Conway, J. D. Harper, and P. T. Lansbury, Jr., Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid, Biochemistry 39, 2552–2563 (2000).
M. A. Speed, D. I. C. Wang, and J. King, Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition, Nature Biotech. 14, 1283–1287 (1996).
B. Schuler, R. Rachel, and R. Seckler, Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike β-helix domain, J. Biol. Chem. 274, 18589–18596 (1999).
D. T. Downing and N. D. Lazo, Molecular modelling indicates that the pathological conformations of prion proteins might be beta-helical, Biochem. J. 343 Pt 2, 453–460 (1999).
N. D. Lazo and D. T. Downing, Amyloid fibrils may be assembled from beta-helical protofibrils, Biochemistry 37, 1731–1735 (1998).
Rights and permissions
Copyright information
© 2006 Springer
About this chapter
Cite this chapter
Gage, M.J., Lefebvre, B.G., Robinson, A.S. (2006). Determinants of Protein Folding and Aggregation in P22 Tailspike Protein. In: Misbehaving Proteins. Springer, New York, NY. https://doi.org/10.1007/978-0-387-36063-8_11
Download citation
DOI: https://doi.org/10.1007/978-0-387-36063-8_11
Publisher Name: Springer, New York, NY
Print ISBN: 978-0-387-30508-0
Online ISBN: 978-0-387-36063-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)