title: [Domain structure of CAF1M protein from Yersinia pestis. Structure and the role of various domains].
abstract: The cooperative structure of Caf1M from Yersinia pestis was studied using scanning microcalorimetry, fluorescence, and limited proteolysis. It was shown that, in Caf1M-Hg (a derivative in which the disulfide bond is replaced by an S-Hg-S bond), the first to melt is the N-domain. Then the C-domain melts. After renaturation in a buffer with a low NaCl concentration, only the C-domain is in the native state, and it can be obtained by limited proteolysis. After renaturation in a buffer with a high NaCl concentration, only the N-domain is in the native state, and it can be obtained by limited proteolysis. Both domains have native structure; however, only the N-domain interacts with Cafl (natural substrate for Caf1M).
authors.affiliation: Institute of Biological Instrument Making, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
authors.forename: V M
authors.initials: VM
authors.lastname: Tishchenko
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D015153:Blotting, Western; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D018832:Molecular Chaperones / Q000737:chemistry*; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D015010:Yersinia pestis / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; C070195:CAf1M protein, Yersinia pestis