CAROLYN TESCHKESummaryAffiliation: University of Connecticut Country: USA Publications
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Publications
'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsCarolyn 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...- GroEL/S substrate specificity based on substrate unfolding propensityKristin 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... 
Folding of phage P22 coat protein monomers: kinetic and thermodynamic propertiesEric 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...- Phage P22 procapsids equilibrate with free coat protein subunitsKristin N Parent
University of Connecticut, Department of Molecular and Cell Biology, Storrs, CT 06269 3125, USA
J Mol Biol 365:513-22. 2007.... - Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switchingKristin 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... - Quantitative analysis of multi-component spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsidsKristin 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... - A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivoKristin 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... - A concerted mechanism for the suppression of a folding defect through interactions with chaperonesShannon 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... - Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroELShannon 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... - Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switchingMargaret 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... - Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assemblyKristin 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... - Penton release from P22 heat-expanded capsids suggests importance of stabilizing penton-hexon interactions during capsid maturationCarolyn 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... - SecA folding kinetics: a large dimeric protein rapidly forms multiple native statesShannon 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 Grants
- Function of SecA2 in Mycobacterium tuberculosis protein exportCAROLYN TESCHKE; Fiscal Year: 2007..In order to develop logical targets for new drugs, the physiology of Mycobacteria must be better understood. ..
- Mechanism of phage P22 assembly, a model dsDNA virusCAROLYN TESCHKE; Fiscal Year: 2007..In addition, these studies will highlight the important interactions between capsid subunits, which are required for proper assembly of viruses. ..
- FOLDING OF PHAGE P22 STRUCTURAL PROTEINSCAROLYN 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. ..
- Mechanism of phage P22 assembly, a model dsDNA virusCarolyn 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. ..