Literature DB >> 8282689

Isolation of suppressors of temperature-sensitive folding mutations.

R Villafane1, A Fleming, C Haase-Pettingell.   

Abstract

Mutations in the tailspike gene (gene 9) of Salmonella typhimurium phage P22 have been used to identify amino acid interactions during the folding of a polypeptide chain. Since temperature-sensitive folding (tsf) mutations cause folding defects in the P22 tailspike polypeptide chain, it is likely that mutants derived from these and correcting the original tsf defects (second-site intragenic suppressors) identify interactions during the folding pathway. We report the isolation and identification of second-site revertants to tsf mutants.

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Year:  1994        PMID: 8282689      PMCID: PMC205024          DOI: 10.1128/jb.176.1.137-142.1994

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  33 in total

1.  Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein.

Authors:  B Fane; R Villafane; A Mitraki; J King
Journal:  J Biol Chem       Date:  1991-06-25       Impact factor: 5.157

2.  Intragenic suppression of a capsid assembly-defective P22 tailspike mutation.

Authors:  P A Maurides; J J Schwarz; P B Berget
Journal:  Genetics       Date:  1990-08       Impact factor: 4.562

Review 3.  Genetic studies of protein stability and mechanisms of folding.

Authors:  D P Goldenberg
Journal:  Annu Rev Biophys Biophys Chem       Date:  1988

Review 4.  Mechanisms of suppression.

Authors:  P E Hartman; J R Roth
Journal:  Adv Genet       Date:  1973       Impact factor: 1.944

Review 5.  Protein engineering. The design, synthesis and characterization of factitious proteins.

Authors:  W V Shaw
Journal:  Biochem J       Date:  1987-08-15       Impact factor: 3.857

6.  Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation.

Authors:  C A Haase-Pettingell; J King
Journal:  J Biol Chem       Date:  1988-04-05       Impact factor: 5.157

7.  Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase.

Authors:  M H Yu; J King
Journal:  Proc Natl Acad Sci U S A       Date:  1984-11       Impact factor: 11.205

8.  Ion-pairs in proteins.

Authors:  D J Barlow; J M Thornton
Journal:  J Mol Biol       Date:  1983-08-25       Impact factor: 5.469

9.  Structure and functions of the bacteriophage P22 tail protein.

Authors:  P B Berget; A R Poteete
Journal:  J Virol       Date:  1980-04       Impact factor: 5.103

10.  Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail-spike protein. I. Fine-structure mapping.

Authors:  D H Smith; P B Berget; J King
Journal:  Genetics       Date:  1980-10       Impact factor: 4.562

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  1 in total

Review 1.  Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.

Authors:  J King; C Haase-Pettingell; A S Robinson; M Speed; A Mitraki
Journal:  FASEB J       Date:  1996-01       Impact factor: 5.191

  1 in total

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