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 bin

SUBMITTER: Tanaka K 

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

REPOSITORIES: biostudies-literature