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tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP: mechanistic and evolutionary implications.

Author(s): Blais SP, Kornblatt JA, Barbeau X, Bonnaure G, Lagüe P, Chênevert R, Lapointe J

PLoS One. 2015;10(4):e0121043 Authors: Blais SP, Kornblatt JA, Barbeau X, Bonnaure G, Lagüe P, Chênevert R, Lapointe J

Article GUID: 25860020
The Energetics of Streptococcal Enolase Octamer Formation: The Quantitative Contributions of the Last Eight Amino Acids at the Carboxy-Terminus.

Author(s): Kornblatt JA, Quiros V, Kornblatt MJ

PLoS One. 2015;10(8):e0135754 Authors: Kornblatt JA, Quiros V, Kornblatt MJ

Article GUID: 26287818
The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.

Author(s): Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

PLoS One. 2014;9(2):e88395 Authors: Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

Article GUID: 24520380
The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen.

Author(s): Deshmukh SS, Kornblatt MJ, Kornblatt JA

PLoS One. 2019;14(1):e0206338 Authors: Deshmukh SS, Kornblatt MJ, Kornblatt JA

Article GUID: 30653526
Title:The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.
Authors:Balhara V,  Deshmukh SS,  Kálmán L,  Kornblatt JA
Link:https://www.ncbi.nlm.nih.gov/pubmed/24520380?dopt=Abstract
Category:PLoS One
PMID:24520380
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, Montréal, Quebec, Canada.
2 Department of Physics, Concordia University, Montréal, Quebec, Canada.
3 Department of Biology and the Centre for Structural and Functional Genomics, Concordia University, Montréal, Quebec, Canada.

Description:

The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.

PLoS One. 2014;9(2):e88395

Authors: Balhara V, Deshmukh SS, Kálmán L, Kornblatt JA

Abstract

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.

PMID: 24520380 [PubMed - indexed for MEDLINE]