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• W2030959635 abstract "Two fundamental properties of monomeric actin were examined in this study, ie its interaction with DNase-I, and the inhibition of endonuclease activity consecutive to the association of the two molecules. In particular, the topological independence between catalytic site of DNase-I and interface with actin, structural changes in actin monomer and the absence of conformational changes in DNase-I were described. We demonstrated a loss of flexibility of antigenic structures in actin subdomain I (ie epitopes 18-28 and 95-105) as well as modification in the exposure of Cys10 and Cys374 after DNase-I binding. Furthermore, the conformational changes induced by DNase-I into the actin molecule weakened the interaction of CapZ to its binding site located in the C-terminal region of actin monomer. These structural changes were time-dependent. When actin was cleaved in the DNase-I binding loop (sequence 38-52) at position 42 by E coli A2 strain protease, a tight DNase-I binding to split actin and the conformational changes were still observed, whereas the DNase-I inhibition activity was completely abolished. Finally, when we substitute Ca2+ by Mg2+ (ATP-Mg2+ monomeric actin) which induces a tighter conformation of actin and partially restores the inhibitory ability of split actin, long-range conformational effects of DNase-I are prevented and the ternary complex DNase-I-actin-CapZ is obtained." @default.
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• W2030959635 date "1997-09-01" @default.
• W2030959635 modified "2023-09-26" @default.
• W2030959635 title "Analysis of long-range structural effects induced by DNase-I interaction with actin monomeric form or complexed to CapZ" @default.
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• W2030959635 doi "https://doi.org/10.1016/s0300-9084(97)82740-x" @default.
• W2030959635 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9451449" @default.
• W2030959635 hasPublicationYear "1997" @default.
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