RRC ID 39658
Author Watanabe-Nakayama T, Itami M, Kodera N, Ando T, Konno H.
Title High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils.
Journal Sci Rep
Abstract Bacterial collagenases involved in donor infection are widely applied in many fields due to their high activity and specificity; however, little is known regarding the mechanisms by which bacterial collagenases degrade insoluble collagen in host tissues. Using high-speed atomic force microscopy, we simultaneously visualized the hierarchical structure of collagen fibrils and the movement of a representative bacterial collagenase, Clostridium histolyticum type I collagenase (ColG), to determine the relationship between collagen structure and collagenase movement. Notably, ColG moved ~14.5 nm toward the collagen N terminus in ~3.8 s in a manner dependent on a catalytic zinc ion. While ColG was engaged, collagen molecules were not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils. Importantly, we found a similarity of relationship between the enzyme-substrate interface structure and enzyme migration in collagen-collagenase and DNA-nuclease systems, which share a helical substrate structure, suggesting a common strategy in enzyme evolution.
Volume 6
Pages 28975
Published 2016-7-4
DOI 10.1038/srep28975
PII srep28975
PMID 27373458
PMC PMC4931465
MeSH Clostridium histolyticum / enzymology* Coenzymes / metabolism Collagen / metabolism* Microbial Collagenase / metabolism* Microscopy, Atomic Force Proteolysis Zinc / metabolism
IF 3.998
Times Cited 12
DNA material Genomic DNA of Clostridium histolyticum JCM 1403T (JGD08942)
General Microbes