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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 influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen.
Authors:Deshmukh SS,  Kornblatt MJ,  Kornblatt JA
Link:https://www.ncbi.nlm.nih.gov/pubmed/30653526?dopt=Abstract
Category:PLoS One
PMID:30653526
Dept Affiliation: BIOLOGY
1 Department of Physics, Concordia University, Montreal Qc, Canada.
2 Department of Chemistry and Biochemistry, Concordia University, Montreal Qc, Canada.
3 Department of Biology, Concordia University, Montreal Qc, Canada.

Description:

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

PLoS One. 2019;14(1):e0206338

Authors: Deshmukh SS, Kornblatt MJ, Kornblatt JA

Abstract

The native octameric structure of streptococcal enolase from Streptococcus pyogenes increasingly dissociates as amino acid residues are removed one by one from the carboxy-terminus. These truncations gradually convert native octameric enolase into monomers and oligomers. In this work, we investigated how these truncations influence the interaction between Streptococcal enolase and canine plasminogen. We used dual polarization interferometry (DPI), localized surface plasmon resonance (LSPR), and sedimentation velocity analytical ultracentrifugation (AUC) to study the interaction. The DPI was our first technique, was performed on all the truncations and used one exclusive kind of chip. The LSRP was used to show that the DPI results were not dependent on the type of chip used. The AUC was required to show that our surface results were not the result of selecting a minority population in any given sample; the majority of the protein was responsible for the binding phenomenon we observed. By comparing results from these techniques we identified one detail that is essential for streptococcal enolase to bind plasminogen: In our hands the individual monomers bind plasminogen; dimers, trimers, tetramers may or may not bind, the fully intact, native, octamer does not bind plasminogen. We also evaluated the contribution to the equilibrium constant made by surface binding as well as in solution. On a surface, the association coefficient is about twice that in solution. The difference is probably not significant. Finally, the fully octameric form of the protein that does not contain a hexa-his N-terminal peptide does not bind to a silicon oxynitride surface, does not bind to an Au-nanoparticle surface, does not bind to a surface coated with Ni-NTA nor does it bind to a surface coated with DPgn. The likelihood is great that the enolase species on the surface of Streptococcus pyogenes is an x-mer of the native octamer.

PMID: 30653526 [PubMed - in process]