Polymerized (F-) actin is induced to form bundles by a number of polycations including
divalent metal ions, Co (NH), and basic polypeptides. The general features of bundle …

A number of positively charged polypeptides and proteins bundle DNA, F-actin,
microtubules, and viruses such as filamentous phage fd and tobacco mosaic virus (TMV), as …

Actin contains a single high-affinity cation-binding site, for which Ca2+ and Mg2+ can
compete, and multiple low-affinity cation-binding sites, which can bind Ca2+, Mg2+, or K+ …

Great effort has been spent in recent years on the investigation of certain aspects of actin
polymerization, such as the dephosphorylation of adenosine triphosphate during G to F …

Actin is known to undergo reversible monomer-polymer transitions that coincide with various
cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This …

We have used N, N'-1, 4-phenylenebismaleimide, a bifunctional sulfhydryl cross-linking
reagent, to probe the oligomeric state of actin during the early stages of its polymerization …

Actin monomers with bound ATP, ADP, or fluorescent analogues of these nucleotides
exchange the nucleotide on a second time scale, whereas filaments assembled from each of …

The assembly of highly purified actin from Dictyostelium discoideum amoebae and rabbit
skeletal muscle by physiological concentrations of KCI proceeds through successive stages …

A large body of biochemical evidence suggests that the F-actin filament can have internal
cooperativity. We have observed large cooperative effects on the low-resolution structure of …

Actin filaments exist in three spatial arrays in cells: single filaments, meshworks or isotropic
gels, and bundles. The formation of actin meshworks or bundles requires the presence of …