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


ABSTRACT: 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.

SUBMITTER: Tanaka K 

PROVIDER: S-EPMC6168687 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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The C-terminal segment of collagenase in <i>Grimontia hollisae</i> binds collagen to enhance collagenolysis.

Tanaka Keisuke K   Teramura Naoko N   Hayashida Osamu O   Iijima Katsumasa K   Okitsu Teru T   Hattori Shunji S  

FEBS open bio 20180906 10


The collagenase secreted by <i>Grimontia hollisae</i> 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 <i>Hathewaya histolytica</i> (<i>Clostridium histolyticum</i>) collagenases; these CBDs a  ...[more]

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