ArticlePloS one2010
Dissociation of the octameric enolase from S. pyogenes--one interface stabilizes another.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Identification of plasminogen-binding sites inFrontiers in cellular and infection microbiology · 2024Article
- Dramatic Changes in Oligomerization Property Caused by Single Residue Deletion in Staphylococcus aureus Enolase.Molecular biotechnology · 2021Article
- Article
- Use of Cyclodextrin as a Novel Agent in the SEC-HPLC Mobile Phase to Mitigate the Interactions of Proteins or Peptide or their Impurities with the Residual Silanols of Commercial SEC-HPLC Columns with Improved Separation and Resolution.Pharmaceutical research · 2018Article
- Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase.PloS one · 2015Article
- Article
- The interaction of streptococcal enolase with canine plasminogen: the role of surfaces in complex formation.PloS one · 2014Article
- An octamer of enolase from Streptococcus suis.Protein & cell · 2012Article
- Surface-affinity profiling to identify host-pathogen interactions.Infection and immunity · 2011Article
- Article
- The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studies.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most enolases are homodimers. There are a few that are octamers, with the eight subunits arranged as a tetramer of dimers. These dimers have the same basic fold and same subunit interactions as are found in the dimeric enolases. The dissociation of the octameric enolase from S. pyogenes was examined, using NaClO(4), a weak chaotrope, to perturb the quaternary structure. Dissociation was monitored by sedimentation velocity. NaClO(4) dissociated the octamer into inactive monomers. There was no indication that dissociation of the octamer into monomers proceeded via formation of significant amounts of dimer or any other intermediate species. Two mutations at the dimer-dimer interface, F137L and E363G, were introduced in order to destabilize the octameric structure. The double mutant was more easily dissociated than was the wild type. Dissociation could also be produced by other salts, including tetramethylammonium chloride (TMACl) or by increasing pH. In all cases, no significant amounts of dimers or other intermediates were formed. Weakening one interface in this protein weakened the other interface as well. Although enolases from most organisms are dimers, the dimeric form of the S. pyogenes enzyme appears to be unstable.
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Registered trials
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