Abstract:
:Collagenase H (ColH) from Clostridium histolyticum is a multimodular protein composed of a collagenase module (activator and peptidase domains), two polycystic kidney disease-like domains, and a collagen-binding domain. The interdomain conformation and its changes are very important for understanding the functions of ColH. In this study, small angle x-ray scattering and limited proteolysis were employed to reveal the interdomain arrangement of ColH in solution. The ab initio beads model indicated that ColH adopted a tapered shape with a swollen head. Under calcium-chelated conditions (with EGTA), the overall structure was further elongated. The rigid body model indicated that the closed form of the collagenase module was preferred in solution. The limited proteolysis demonstrated that the protease sensitivity of ColH was significantly increased under the calcium-chelated conditions, and that the digestion mainly occurred in the domain linker regions. Fluorescence measurements with a fluorescent dye were performed with the limited proteolysis products after separation. The results indicated that the limited proteolysis products exhibited fluorescence similar to that of the full-length ColH. These findings suggested that the conformation of full-length ColH in solution is the elongated form, and this form is calcium-dependently maintained at the domain linker regions.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Ohbayashi N,Matsumoto T,Shima H,Goto M,Watanabe K,Yamano A,Katoh Y,Igarashi K,Yamagata Y,Murayama Kdoi
10.1016/j.bpj.2013.02.022subject
Has Abstractpub_date
2013-04-02 00:00:00pages
1538-45issue
7eissn
0006-3495issn
1542-0086pii
S0006-3495(13)00239-7journal_volume
104pub_type
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