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The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis

The collagenase secreted by Grimontia hollisae strain 1706B is a 74 kDa protein that consists of two parts: the catalytic module and a C‐terminal segment that includes the bacterial pre‐peptidase C‐terminal domain. Here, we produced a recombinant C‐terminal segment protein and examined its ability t...

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Autores principales: Tanaka, Keisuke, Teramura, Naoko, Hayashida, Osamu, Iijima, Katsumasa, Okitsu, Teru, Hattori, Shunji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6168687/
https://www.ncbi.nlm.nih.gov/pubmed/30338219
http://dx.doi.org/10.1002/2211-5463.12510
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author Tanaka, Keisuke
Teramura, Naoko
Hayashida, Osamu
Iijima, Katsumasa
Okitsu, Teru
Hattori, Shunji
author_facet Tanaka, Keisuke
Teramura, Naoko
Hayashida, Osamu
Iijima, Katsumasa
Okitsu, Teru
Hattori, Shunji
author_sort Tanaka, Keisuke
collection PubMed
description The collagenase secreted by Grimontia hollisae strain 1706B is a 74 kDa protein that consists of two parts: the catalytic module and a C‐terminal segment that includes the bacterial pre‐peptidase C‐terminal domain. Here, we produced a recombinant C‐terminal segment protein and examined its ability to bind collagen and other characteristics as compared with collagen‐binding domains (CBDs) derived from Hathewaya histolytica (Clostridium histolyticum) collagenases; these CBDs are the only ones thus far identified in bacterial collagenases. We found that the C‐terminal segment binds to collagen only when the collagen is in its triple‐helical conformation. Moreover, the C‐terminal segment and the CBDs from H. histolytica have comparable characteristics, including binding affinity to type I collagen, substrate spectrum, and binding conditions with respect to salt concentration and pH. However, the C‐terminal segment has a completely different primary structure from those of the CBDs from H. histolytica. As regards secondary structure, in silico prediction indicates that the C‐terminal segment may be homologous to those in CBDs from H. histolytica. Furthermore, we performed collagenase assays using fluorescein isothiocyanate‐labeled type I collagen to show that the C‐terminal segment positively contributes to the collagenolytic activity of the 74 kDa collagenase from G. hollisae.
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spelling pubmed-61686872018-10-18 The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis Tanaka, Keisuke Teramura, Naoko Hayashida, Osamu Iijima, Katsumasa Okitsu, Teru Hattori, Shunji FEBS Open Bio Research Articles The collagenase secreted by Grimontia hollisae strain 1706B is a 74 kDa protein that consists of two parts: the catalytic module and a C‐terminal segment that includes the bacterial pre‐peptidase C‐terminal domain. Here, we produced a recombinant C‐terminal segment protein and examined its ability to bind collagen and other characteristics as compared with collagen‐binding domains (CBDs) derived from Hathewaya histolytica (Clostridium histolyticum) collagenases; these CBDs are the only ones thus far identified in bacterial collagenases. We found that the C‐terminal segment binds to collagen only when the collagen is in its triple‐helical conformation. Moreover, the C‐terminal segment and the CBDs from H. histolytica have comparable characteristics, including binding affinity to type I collagen, substrate spectrum, and binding conditions with respect to salt concentration and pH. However, the C‐terminal segment has a completely different primary structure from those of the CBDs from H. histolytica. As regards secondary structure, in silico prediction indicates that the C‐terminal segment may be homologous to those in CBDs from H. histolytica. Furthermore, we performed collagenase assays using fluorescein isothiocyanate‐labeled type I collagen to show that the C‐terminal segment positively contributes to the collagenolytic activity of the 74 kDa collagenase from G. hollisae. John Wiley and Sons Inc. 2018-09-06 /pmc/articles/PMC6168687/ /pubmed/30338219 http://dx.doi.org/10.1002/2211-5463.12510 Text en © 2018 Nippi Research Institute of Biomatrix. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Tanaka, Keisuke
Teramura, Naoko
Hayashida, Osamu
Iijima, Katsumasa
Okitsu, Teru
Hattori, Shunji
The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis
title The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis
title_full The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis
title_fullStr The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis
title_full_unstemmed The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis
title_short The C‐terminal segment of collagenase in Grimontia hollisae binds collagen to enhance collagenolysis
title_sort c‐terminal segment of collagenase in grimontia hollisae binds collagen to enhance collagenolysis
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6168687/
https://www.ncbi.nlm.nih.gov/pubmed/30338219
http://dx.doi.org/10.1002/2211-5463.12510
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