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The ** N **‐terminal fragment of gelsolin inhibits the interaction of DNase I with isolated actin, but not with the cofilin‐actin complex by Deepak Chhabra; Neil J. Nosworthy; Cristobal G. dos Remedios is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Apoptosis is essential in embryonic development, clonal selection of cells of the immune system and in the prevention of cancer. Apoptotic cells display characteristic changes in morphology that precede the eventual fragmentation of nuclear DNA resulting in cell death. Current evidence implicates DNase I as responsible for hydrolysis of DNA during apoptosis. __In vivo__, it is likely that cytoplasmic actin binds and inhibits the enzymatic activity and nuclear translocation of DNase I and that disruption of the actin–DNase I complex results in activation of DNase I. In this report we demonstrate that the __N__‐terminal fragment of gelsolin (__N__‐gelsolin) disrupts the actin–DNase I interaction. This provides a molecular mechanism for the role of the __N__‐gelsolin in regulating DNase I activity. We also show that cofilin stabilises the actin–DNase I complex by forming a ternary complex that prevents __N__‐gelsolin from releasing DNase I from actin. We suggest that both cofilin and gelsolin are essential in modulating the release of DNase I from actin.

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Author

Deepak Chhabra; Neil J. Nosworthy; Cristobal G. dos Remedios

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)