What is the structure of the RecA-DNA filament?

The bacterial RecA protein has been a model system for understanding how a protein can catalyze homologous genetic recombination. RecA-like proteins have now been characterized from many organisms, from bacteriophage to humans. Some of the RecA-like proteins, including human RAD51, appear to function as helical filaments formed on DNA.

ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments.

Proteins in the ADF/cofilin (AC) family are essential for rapid rearrangements of cellular actin structures. They have been shown to be active in both the severing and depolymerization of actin filaments in vitro, but the detailed mechanism of action is not known. Under in vitro conditions, subunits in the actin filament can treadmill; with the hydrolysis of ATP driving the addition of subunits at one end of the filament and loss of subunits from the opposite end.

Complexes of RecA with LexA and RecX differentiate between active and inactive RecA nucleoprotein filaments.

The bacterial RecA protein has been the dominant model system for understanding homologous genetic recombination. Although a crystal structure of RecA was solved ten years ago, we still do not have a detailed understanding of how the helical filament formed by RecA on DNA catalyzes the recognition of homology and the exchange of strands between two DNA molecules. Recent structural and spectroscopic studies have suggested that subunits in the helical filament formed in the RecA crystal are rotated when compared to the active RecA-ATP-DNA filament.

Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms.

Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen.

Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?

Tandem calponin-homology (CH) domains play an important role in the actin-binding function of many spectrin superfamily proteins. Crystal structures from several of these proteins have suggested a flexibility between these domains, and the manner in which these domains bind to F-actin has been the subject of some controversy. A recent paper has used electron microscopy and three-dimensional reconstruction to examine the complex of the utrophin tandem CH domain with F-actin.