Biochemical characterisation of a collagenase from Bacillus cereus strain Q1

Abstract Collagen is the most abundant protein in higher animals and as such it is a valuable source of amino acids and carbon for saprophytic bacteria. Due to its unique amino acid composition and triple-helical tertiary structure it can however only be cleaved by specialized proteases like the col...

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Autores principales:	Isabel J. Hoppe, Hans Brandstetter, Esther Schönauer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/30fffa4204a048ce98ae70b6bfba59b5
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spelling	oai:doaj.org-article:30fffa4204a048ce98ae70b6bfba59b52021-12-02T14:03:46ZBiochemical characterisation of a collagenase from Bacillus cereus strain Q110.1038/s41598-021-83744-62045-2322https://doaj.org/article/30fffa4204a048ce98ae70b6bfba59b52021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83744-6https://doaj.org/toc/2045-2322Abstract Collagen is the most abundant protein in higher animals and as such it is a valuable source of amino acids and carbon for saprophytic bacteria. Due to its unique amino acid composition and triple-helical tertiary structure it can however only be cleaved by specialized proteases like the collagenases secreted by some bacteria. Among the best described bacterial collagenases are ColG and ColH from Clostridium histolyticum. Many Bacillus species contain homologues of clostridial collagenases, which play a role in some infections caused by B. cereus. Detailed biochemical and enzymatic characterizations of bacillial collagenases are however lacking at this time. In an effort to close this gap in knowledge we expressed ColQ1 from B. cereus strain Q1 recombinantly, investigated its metal dependency and performed peptide, gelatin and collagen degradation assays. Our results show that ColQ1 is a true collagenase, cleaving natively folded collagen six times more efficiently than ColG while at the same time being a similarly effective peptidase as ColH. In both ColQ1 and ColG the rate-limiting step in collagenolysis is the unwinding of the triple-helix. The data suggest an orchestrated multi-domain mechanism for efficient helicase activity.Isabel J. HoppeHans BrandstetterEsther SchönauerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Isabel J. Hoppe Hans Brandstetter Esther Schönauer Biochemical characterisation of a collagenase from Bacillus cereus strain Q1
description	Abstract Collagen is the most abundant protein in higher animals and as such it is a valuable source of amino acids and carbon for saprophytic bacteria. Due to its unique amino acid composition and triple-helical tertiary structure it can however only be cleaved by specialized proteases like the collagenases secreted by some bacteria. Among the best described bacterial collagenases are ColG and ColH from Clostridium histolyticum. Many Bacillus species contain homologues of clostridial collagenases, which play a role in some infections caused by B. cereus. Detailed biochemical and enzymatic characterizations of bacillial collagenases are however lacking at this time. In an effort to close this gap in knowledge we expressed ColQ1 from B. cereus strain Q1 recombinantly, investigated its metal dependency and performed peptide, gelatin and collagen degradation assays. Our results show that ColQ1 is a true collagenase, cleaving natively folded collagen six times more efficiently than ColG while at the same time being a similarly effective peptidase as ColH. In both ColQ1 and ColG the rate-limiting step in collagenolysis is the unwinding of the triple-helix. The data suggest an orchestrated multi-domain mechanism for efficient helicase activity.
format	article
author	Isabel J. Hoppe Hans Brandstetter Esther Schönauer
author_facet	Isabel J. Hoppe Hans Brandstetter Esther Schönauer
author_sort	Isabel J. Hoppe
title	Biochemical characterisation of a collagenase from Bacillus cereus strain Q1
title_short	Biochemical characterisation of a collagenase from Bacillus cereus strain Q1
title_full	Biochemical characterisation of a collagenase from Bacillus cereus strain Q1
title_fullStr	Biochemical characterisation of a collagenase from Bacillus cereus strain Q1
title_full_unstemmed	Biochemical characterisation of a collagenase from Bacillus cereus strain Q1
title_sort	biochemical characterisation of a collagenase from bacillus cereus strain q1
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/30fffa4204a048ce98ae70b6bfba59b5
work_keys_str_mv	AT isabeljhoppe biochemicalcharacterisationofacollagenasefrombacilluscereusstrainq1 AT hansbrandstetter biochemicalcharacterisationofacollagenasefrombacilluscereusstrainq1 AT estherschonauer biochemicalcharacterisationofacollagenasefrombacilluscereusstrainq1
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Biochemical characterisation of a collagenase from Bacillus cereus strain Q1

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