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The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation
The enolase from Streptococcus pyogenes (Str enolase F137L/E363G) is a homo-octamer shaped like a donut. Plasminogen (Pgn) is a monomeric protein composed of seven discrete separated domains organized into a lock washer. The enolase is known to bind Pgn. In past work we searched for conditions in wh...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919783/ https://www.ncbi.nlm.nih.gov/pubmed/24520380 http://dx.doi.org/10.1371/journal.pone.0088395 |
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author | Balhara, Vinod Deshmukh, Sasmit S. Kálmán, László Kornblatt, Jack A. |
author_facet | Balhara, Vinod Deshmukh, Sasmit S. Kálmán, László Kornblatt, Jack A. |
author_sort | Balhara, Vinod |
collection | PubMed |
description | The enolase from Streptococcus pyogenes (Str enolase F137L/E363G) is a homo-octamer shaped like a donut. Plasminogen (Pgn) is a monomeric protein composed of seven discrete separated domains organized into a lock washer. The enolase is known to bind Pgn. In past work we searched for conditions in which the two proteins would bind to one another. The two native proteins in solution would not bind under any of the tried conditions. We found that if the structures were perturbed binding would occur. We stated that only the non-native Str enolase or Pgn would interact such that we could detect binding. We report here the results of a series of dual polarization interferometry (DPI) experiments coupled with atomic force microscopy (AFM), isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence. We show that the critical condition for forming stable complexes of the two native proteins involves Str enolase binding to a surface. Surfaces that attract Str enolase are a sufficient condition for binding Pgn. Under certain conditions, Pgn adsorbed to a surface will bind Str enolase. |
format | Online Article Text |
id | pubmed-3919783 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39197832014-02-11 The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation Balhara, Vinod Deshmukh, Sasmit S. Kálmán, László Kornblatt, Jack A. PLoS One Research Article The enolase from Streptococcus pyogenes (Str enolase F137L/E363G) is a homo-octamer shaped like a donut. Plasminogen (Pgn) is a monomeric protein composed of seven discrete separated domains organized into a lock washer. The enolase is known to bind Pgn. In past work we searched for conditions in which the two proteins would bind to one another. The two native proteins in solution would not bind under any of the tried conditions. We found that if the structures were perturbed binding would occur. We stated that only the non-native Str enolase or Pgn would interact such that we could detect binding. We report here the results of a series of dual polarization interferometry (DPI) experiments coupled with atomic force microscopy (AFM), isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence. We show that the critical condition for forming stable complexes of the two native proteins involves Str enolase binding to a surface. Surfaces that attract Str enolase are a sufficient condition for binding Pgn. Under certain conditions, Pgn adsorbed to a surface will bind Str enolase. Public Library of Science 2014-02-10 /pmc/articles/PMC3919783/ /pubmed/24520380 http://dx.doi.org/10.1371/journal.pone.0088395 Text en © 2014 Balhara et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Balhara, Vinod Deshmukh, Sasmit S. Kálmán, László Kornblatt, Jack A. The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation |
title | The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation |
title_full | The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation |
title_fullStr | The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation |
title_full_unstemmed | The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation |
title_short | The Interaction of Streptococcal Enolase with Canine Plasminogen: The Role of Surfaces in Complex Formation |
title_sort | interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919783/ https://www.ncbi.nlm.nih.gov/pubmed/24520380 http://dx.doi.org/10.1371/journal.pone.0088395 |
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