CAROLYN TESCHKE

Summary

Affiliation: University of Connecticut
Country: USA

Publications

  1. pmc 'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants
    Carolyn M Teschke
    Department of Molecular and Cell Biology, 91 N Eagleville Rd, U 3125, University of Connecticut, Storrs, CT 06269 3125, USA
    Virology 401:119-30. 2010
  2. pmc GroEL/S substrate specificity based on substrate unfolding propensity
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA
    Cell Stress Chaperones 12:20-32. 2007
  3. ncbi request reprint Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties
    Eric Anderson
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    Virology 313:184-97. 2003
  4. pmc Phage P22 procapsids equilibrate with free coat protein subunits
    Kristin N Parent
    University of Connecticut, Department of Molecular and Cell Biology, Storrs, CT 06269 3125, USA
    J Mol Biol 365:513-22. 2007
  5. pmc Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA
    Mol Microbiol 65:1300-10. 2007
  6. ncbi request reprint Quantitative analysis of multi-component spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsids
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    J Mol Biol 359:1097-106. 2006
  7. ncbi request reprint A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    Mol Microbiol 54:1036-50. 2004
  8. ncbi request reprint A concerted mechanism for the suppression of a folding defect through interactions with chaperones
    Shannon M Doyle
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269 3125, USA
    J Biol Chem 279:17473-82. 2004
  9. ncbi request reprint Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL
    Shannon M Doyle
    Department of Molecular and Cell Biology, University of Connecticut, 91 N Eagleville Road, Storrs, CT 06269 3125, USA
    J Mol Biol 332:937-51. 2003
  10. pmc Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching
    Margaret M Suhanovsky
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA
    Mol Microbiol 77:1568-82. 2010

Research Grants

  1. Function of SecA2 in Mycobacterium tuberculosis protein export
    CAROLYN TESCHKE; Fiscal Year: 2007
  2. Mechanism of phage P22 assembly, a model dsDNA virus
    CAROLYN TESCHKE; Fiscal Year: 2007
  3. FOLDING OF PHAGE P22 STRUCTURAL PROTEINS
    CAROLYN TESCHKE; Fiscal Year: 2003
  4. Mechanism of phage P22 assembly, a model dsDNA virus
    Carolyn M Teschke; Fiscal Year: 2010

Collaborators

  • A Zlotnick
  • Kristin N Parent
  • Shannon M Doyle
  • Margaret M Suhanovsky
  • Eric Anderson
  • Timothy S Baker
  • Sarah E Dunn
  • Matthew J Ranaghan
  • Osman Bilsel
  • Dan Zhu
  • Emory H Braswell

Detail Information

Publications13

  1. pmc 'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants
    Carolyn M Teschke
    Department of Molecular and Cell Biology, 91 N Eagleville Rd, U 3125, University of Connecticut, Storrs, CT 06269 3125, USA
    Virology 401:119-30. 2010
    ..Here we highlight the pseudo-atomic structures of phage P22 coat protein and rationalize several decades of data about P22 coat protein folding, assembly and maturation generated from a combination of genetics and biochemistry...
  2. pmc GroEL/S substrate specificity based on substrate unfolding propensity
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA
    Cell Stress Chaperones 12:20-32. 2007
    ..Our data also suggest that GroEL/S can be induced by increasing the population of unfolding intermediates...
  3. ncbi request reprint Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties
    Eric Anderson
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    Virology 313:184-97. 2003
    ..Additionally, two native states were identified, suggesting that the several conformers required to assemble an icosahedral capsid may be found in solution before assembly ensues...
  4. pmc Phage P22 procapsids equilibrate with free coat protein subunits
    Kristin N Parent
    University of Connecticut, Department of Molecular and Cell Biology, Storrs, CT 06269 3125, USA
    J Mol Biol 365:513-22. 2007
    ....
  5. pmc Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA
    Mol Microbiol 65:1300-10. 2007
    ..Our results suggest that a previously identified surface-exposed loop in coat protein is critical in conformational switching of subunits during both procapsid assembly and maturation...
  6. ncbi request reprint Quantitative analysis of multi-component spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsids
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    J Mol Biol 359:1097-106. 2006
    ..When the relative concentration is very high, too many nuclei form, leading to kinetically trapped assembly intermediates...
  7. ncbi request reprint A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo
    Kristin N Parent
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    Mol Microbiol 54:1036-50. 2004
    ..Through more proficient use of this chaperone network, the su substitutions exhibit a novel means of suppression of a folding defect...
  8. ncbi request reprint A concerted mechanism for the suppression of a folding defect through interactions with chaperones
    Shannon M Doyle
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269 3125, USA
    J Biol Chem 279:17473-82. 2004
    ..Thus, the suppressor substitution likely improves folding in vivo through increased efficiency of coat protein-chaperone interactions...
  9. ncbi request reprint Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL
    Shannon M Doyle
    Department of Molecular and Cell Biology, University of Connecticut, 91 N Eagleville Road, Storrs, CT 06269 3125, USA
    J Mol Biol 332:937-51. 2003
    ..Thus, the tsf coat proteins aggregate in vivo because of an increased propensity to populate this unfolding intermediate...
  10. pmc Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching
    Margaret M Suhanovsky
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, USA
    Mol Microbiol 77:1568-82. 2010
    ..Thus, correct coat protein interactions with scaffolding protein and maintenance of sufficient coat protein flexibility are crucial for proper P22 assembly. The coat protein β-hinge region is the major determinant for both features...
  11. ncbi request reprint Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly
    Kristin N Parent
    Department of Molecular and Cell Biology, Unit 3125, University of Connecticut, Storrs, CT 06269 3125, USA
    Virology 340:33-45. 2005
    ..We hypothesize that low salt conditions increase the coat protein:scaffolding protein affinity, causing excessive nuclei to form, which decreases coat protein levels leading to incomplete assembly...
  12. pmc Penton release from P22 heat-expanded capsids suggests importance of stabilizing penton-hexon interactions during capsid maturation
    Carolyn M Teschke
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269, USA
    Biophys J 84:2585-92. 2003
    ..When considered in the context of other studies using chemical or heat treatment of capsids, our study indicates that penton release may be a common trend among double-stranded DNA containing viruses...
  13. ncbi request reprint SecA folding kinetics: a large dimeric protein rapidly forms multiple native states
    Shannon M Doyle
    Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269 3125, USA
    J Mol Biol 341:199-214. 2004
    ..These results confirm that SecA is a highly dynamic protein, consistent with the rapid, major conformational changes it must undergo in vivo...

Research Grants11

  1. Function of SecA2 in Mycobacterium tuberculosis protein export
    CAROLYN TESCHKE; Fiscal Year: 2007
    ..In order to develop logical targets for new drugs, the physiology of Mycobacteria must be better understood. ..
  2. Mechanism of phage P22 assembly, a model dsDNA virus
    CAROLYN TESCHKE; Fiscal Year: 2007
    ..In addition, these studies will highlight the important interactions between capsid subunits, which are required for proper assembly of viruses. ..
  3. FOLDING OF PHAGE P22 STRUCTURAL PROTEINS
    CAROLYN TESCHKE; Fiscal Year: 2003
    ..The range of approaches will allow insight into the factors which control protein folding and assembly in vivo. This insight is important since misfolding and/or protein misassembly has been implicated in serious diseases. ..
  4. Mechanism of phage P22 assembly, a model dsDNA virus
    Carolyn M Teschke; Fiscal Year: 2010
    ..In addition, these studies will highlight the important interactions between capsid subunits, which are required for proper assembly of viruses. ..