Construction of a xylanase A variant capable of polymerization.

The aim of our work is to furnish enzymes with polymerization ability by creating fusion constructs with the polymerizable protein, flagellin, the main component of bacterial flagellar filaments. The D3 domain of flagellin, exposed on the surface of flagellar filaments, is formed by the hypervariabl...

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Autores principales:	Veronika Szabó, Adél Muskotál, Balázs Tóth, Marko D Mihovilovic, Ferenc Vonderviszt
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/66b69c99d41d4ce388b87bd625e4071f
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spelling	oai:doaj.org-article:66b69c99d41d4ce388b87bd625e4071f2021-11-04T06:07:52ZConstruction of a xylanase A variant capable of polymerization.1932-620310.1371/journal.pone.0025388https://doaj.org/article/66b69c99d41d4ce388b87bd625e4071f2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21966517/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The aim of our work is to furnish enzymes with polymerization ability by creating fusion constructs with the polymerizable protein, flagellin, the main component of bacterial flagellar filaments. The D3 domain of flagellin, exposed on the surface of flagellar filaments, is formed by the hypervariable central portion of the polypeptide chain. D3 is not essential for filament formation. The concept in this project is to replace the D3 domain with suitable monomeric enzymes without adversely affecting polymerization ability, and to assemble these chimeric flagellins into tubular nanostructures. To test the feasibility of this approach, xylanase A (XynA) from B. subtilis was chosen as a model enzyme for insertion into the central part of flagellin. With the help of genetic engineering, a fusion construct was created in which the D3 domain was replaced by XynA. The flagellin-XynA chimera exhibited catalytic activity as well as polymerization ability. These results demonstrate that polymerization ability can be introduced into various proteins, and building blocks for rationally designed assembly of filamentous nanostructures can be created.Veronika SzabóAdél MuskotálBalázs TóthMarko D MihovilovicFerenc VondervisztPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 9, p e25388 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Veronika Szabó Adél Muskotál Balázs Tóth Marko D Mihovilovic Ferenc Vonderviszt Construction of a xylanase A variant capable of polymerization.
description	The aim of our work is to furnish enzymes with polymerization ability by creating fusion constructs with the polymerizable protein, flagellin, the main component of bacterial flagellar filaments. The D3 domain of flagellin, exposed on the surface of flagellar filaments, is formed by the hypervariable central portion of the polypeptide chain. D3 is not essential for filament formation. The concept in this project is to replace the D3 domain with suitable monomeric enzymes without adversely affecting polymerization ability, and to assemble these chimeric flagellins into tubular nanostructures. To test the feasibility of this approach, xylanase A (XynA) from B. subtilis was chosen as a model enzyme for insertion into the central part of flagellin. With the help of genetic engineering, a fusion construct was created in which the D3 domain was replaced by XynA. The flagellin-XynA chimera exhibited catalytic activity as well as polymerization ability. These results demonstrate that polymerization ability can be introduced into various proteins, and building blocks for rationally designed assembly of filamentous nanostructures can be created.
format	article
author	Veronika Szabó Adél Muskotál Balázs Tóth Marko D Mihovilovic Ferenc Vonderviszt
author_facet	Veronika Szabó Adél Muskotál Balázs Tóth Marko D Mihovilovic Ferenc Vonderviszt
author_sort	Veronika Szabó
title	Construction of a xylanase A variant capable of polymerization.
title_short	Construction of a xylanase A variant capable of polymerization.
title_full	Construction of a xylanase A variant capable of polymerization.
title_fullStr	Construction of a xylanase A variant capable of polymerization.
title_full_unstemmed	Construction of a xylanase A variant capable of polymerization.
title_sort	construction of a xylanase a variant capable of polymerization.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/66b69c99d41d4ce388b87bd625e4071f
work_keys_str_mv	AT veronikaszabo constructionofaxylanaseavariantcapableofpolymerization AT adelmuskotal constructionofaxylanaseavariantcapableofpolymerization AT balazstoth constructionofaxylanaseavariantcapableofpolymerization AT markodmihovilovic constructionofaxylanaseavariantcapableofpolymerization AT ferencvonderviszt constructionofaxylanaseavariantcapableofpolymerization
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Construction of a xylanase A variant capable of polymerization.

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