scholarly journals Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains

2008 ◽  
Vol 4 (5) ◽  
pp. 900-908 ◽  
Author(s):  
Margaret A. Speed ◽  
Daniel I.C. Wang ◽  
Jonathan King
Keyword(s):  
Inclusion Body ◽  
Body State ◽  
P22 Tailspike ◽  
Polypeptide Chains

Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition

1996 ◽  
Vol 14 (10) ◽  
pp. 1283-1287 ◽  
Author(s):  
Margaret A. Speed ◽  
Daniel I. C. Wang ◽  
Jonathan King
Keyword(s):  
Body Composition ◽  
Inclusion Body ◽  
Molecular Basis ◽  
Polypeptide Chains

scholarly journals Intragenic suppressors of folding defects in the P22 tailspike protein.

Genetics ◽  
1991 ◽  
Vol 127 (2) ◽  
pp. 263-277 ◽  
Author(s):  
B Fane ◽  
J King
Keyword(s):  
Amino Acid Sequences ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Chain Folding ◽  
Phage P22 ◽  
Nonsense Codons ◽  
P22 Tailspike ◽  
Polypeptide Chains ◽  
Tailspike Protein

Abstract Within the amino acid sequences of polypeptide chains little is known of the distribution of sites and sequences critical for directing chain folding and assembly. Temperature-sensitive folding (tsf) mutations identifying such sites have been previously isolated and characterized in gene 9 of phage P22 encoding the tailspike endorhamnosidase. We report here the isolation of a set of second-site conformational suppressors which alleviate the defect in such folding mutants. The suppressors were selected for their ability to correct the defects of missense tailspike polypeptide chains, generated by growth of gene 9 amber mutants on Salmonella host strains inserting either tyrosine, serine, glutamine or leucine at the nonsense codons. Second-site suppressors were recovered for 13 of 22 starting sites. The suppressors of defects at six sites mapped within gene 9. (Suppressors for seven other sites were extragenic and distant from gene 9.) The missense polypeptide chains generated from all six suppressible sites displayed ts phenotypes. Temperature-sensitive alleles were isolated at these amber sites by pseudoreversion. The intragenic suppressors restored growth at the restrictive temperature of these presumptive tsf alleles. Characterization of protein maturation in cells infected with mutant phages carrying the intragenic suppressors indicates that the suppression is acting at the level of polypeptide chain folding and assembly.

Periodic Structure in the Matrix Protein of an Insect Virus

1982 ◽  
Vol 40 ◽  
pp. 302-303
Author(s):  
H.M. Mazzone ◽  
W.F. Engler ◽  
R. Zerillo ◽  
G.F. Bahr
Keyword(s):  
Inclusion Body ◽  
Periodic Structure ◽  
Matrix Protein ◽  
Malacosoma Disstria ◽  
Insect Virus ◽  
Virus Particles ◽  
The Matrix ◽  
Nucleopolyhedrosis Virus

The nucleopolyhedrosis virus (NPV) of the forest tent cater - pillar (Malacosoma disstria Hubner) has been analyzed in our laboratories. As a representative of the Baculovirus class, the NPV has virus particles enclosed with in a proteinaceous structure, the inclusion body.

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

Molecular pathogenesis of hereditary inclusion body myopathies

2009 ◽  
Vol 40 (01) ◽  
Author(s):  
S Krause ◽  
N Garcia-Angarita ◽  
A Aleo ◽  
S Hinderlich ◽  
MC Walter ◽  
...  
Keyword(s):  
Inclusion Body ◽  
Molecular Pathogenesis
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