Journal
JOURNAL OF CELL BIOLOGY
Volume 153, Issue 1, Pages 75-86Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.153.1.75
Keywords
actin; ADF; cooperativity; electron microscopy; image processing
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Funding
- NCRR NIH HHS [P41-RR12255] Funding Source: Medline
- NIAMS NIH HHS [R01-AR42023] Funding Source: Medline
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Proteins in the actin depolymerizing factor (ADF)/cofilin family are essential for rapid F-actin turnover, and most depolymerize actin in a pH-dependent manner. Complexes of human and plant ADF with F-actin at different pH were examined using electron microscopy and a novel method of image analysis for helical filaments. Although ADF changes the mean twist of actin, we show that it does this by stabilizing a preexisting F-actin angular conformation. In addition, ADF induces a large (similar to 12 degrees) tilt of actin subunits at high pH where filaments are readily disrupted. A second ADF molecule binds to a site on the opposite side of F-actin from that of the previously described ADF binding site, and this second site is only largely occupied at high pH. All of these states display a high degree of cooperativity that appears to be an integral part of F-actin.
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