Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.

The βγ-crystallin superfamily possesses a large number of versatile members, of which only a few members other than lens βγ-crystallins have been studied. Understanding the non-crystallin functions as well as origin of crystallin-like properties of such proteins is possible by exploring novel member...

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Autores principales:	Shashi Kumar Suman, Daddali Ravindra, Yogendra Sharma, Amita Mishra
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/576d468b60944840bdec80434d47111c
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spelling	oai:doaj.org-article:576d468b60944840bdec80434d47111c2021-11-18T08:00:41ZAssociation properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.1932-620310.1371/journal.pone.0053610https://doaj.org/article/576d468b60944840bdec80434d47111c2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23349723/?tool=EBIhttps://doaj.org/toc/1932-6203The βγ-crystallin superfamily possesses a large number of versatile members, of which only a few members other than lens βγ-crystallins have been studied. Understanding the non-crystallin functions as well as origin of crystallin-like properties of such proteins is possible by exploring novel members from diverse sources. We describe a novel βγ-crystallin domain with S-type (Spherulin 3a type) Greek key motifs in protein vibrillin from a pathogenic bacterium Vibrio cholerae. This domain is a part of a large Vibrio-specific protein prevalent in Vibrio species (found in at least fourteen different strains sequenced so far). The domain contains two canonical N/D-N/D-X-X-S/T-S Ca(2+)-binding motifs, and bind Ca(2+). Unlike spherulin 3a and other microbial homologues studied so far, βγ-crystallin domain of vibrillin self-associates forming oligomers of various sizes including dimers. The fractionated dimers readily form octamers in concentration-dependent manner, suggesting an association between these two major forms. The domain associates/dissociates forming dimers at the cost of monomeric populations in the presence of Ca(2+). No such effect of Ca(2+) has been observed in oligomeric species. The equilibrium unfolding of both forms follows a similar pattern, with the formation of an unfolding intermediate at sub-molar concentrations of denaturant. These properties exhibited by this βγ-crystallin domain are not shown by any other domain studied so far, demonstrating the diversity in domain properties.Shashi Kumar SumanDaddali RavindraYogendra SharmaAmita MishraPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 1, p e53610 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shashi Kumar Suman Daddali Ravindra Yogendra Sharma Amita Mishra Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
description	The βγ-crystallin superfamily possesses a large number of versatile members, of which only a few members other than lens βγ-crystallins have been studied. Understanding the non-crystallin functions as well as origin of crystallin-like properties of such proteins is possible by exploring novel members from diverse sources. We describe a novel βγ-crystallin domain with S-type (Spherulin 3a type) Greek key motifs in protein vibrillin from a pathogenic bacterium Vibrio cholerae. This domain is a part of a large Vibrio-specific protein prevalent in Vibrio species (found in at least fourteen different strains sequenced so far). The domain contains two canonical N/D-N/D-X-X-S/T-S Ca(2+)-binding motifs, and bind Ca(2+). Unlike spherulin 3a and other microbial homologues studied so far, βγ-crystallin domain of vibrillin self-associates forming oligomers of various sizes including dimers. The fractionated dimers readily form octamers in concentration-dependent manner, suggesting an association between these two major forms. The domain associates/dissociates forming dimers at the cost of monomeric populations in the presence of Ca(2+). No such effect of Ca(2+) has been observed in oligomeric species. The equilibrium unfolding of both forms follows a similar pattern, with the formation of an unfolding intermediate at sub-molar concentrations of denaturant. These properties exhibited by this βγ-crystallin domain are not shown by any other domain studied so far, demonstrating the diversity in domain properties.
format	article
author	Shashi Kumar Suman Daddali Ravindra Yogendra Sharma Amita Mishra
author_facet	Shashi Kumar Suman Daddali Ravindra Yogendra Sharma Amita Mishra
author_sort	Shashi Kumar Suman
title	Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
title_short	Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
title_full	Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
title_fullStr	Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
title_full_unstemmed	Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.
title_sort	association properties and unfolding of a βγ-crystallin domain of a vibrio-specific protein.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/576d468b60944840bdec80434d47111c
work_keys_str_mv	AT shashikumarsuman associationpropertiesandunfoldingofabgcrystallindomainofavibriospecificprotein AT daddaliravindra associationpropertiesandunfoldingofabgcrystallindomainofavibriospecificprotein AT yogendrasharma associationpropertiesandunfoldingofabgcrystallindomainofavibriospecificprotein AT amitamishra associationpropertiesandunfoldingofabgcrystallindomainofavibriospecificprotein
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Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific protein.

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