G-actin-tubulin interaction

Treadmilling of tubulin and actin.

Chaperonin-mediated folding of actin and tubulin

T HE central dogma of molecular biology holds that proteins contain within their primary amino acid sequence all the information that is required to dictate their three-dimensional structure. In principle, therefore, proteins can fold spontaneously (2). It is now clear, however, that the proper folding of many proteins requires facilitation. The facilitation reaction is accomplished via interac...

Hsp27-Actin Interaction

Hsp27 oligomer is reported to interact with F-actin as a barbed-end-capping protein. The present study determined the binding strength and stoichiometry of the interaction using fluorescence of probes attached to Hsp27 cysteine-137. The fluorescence of acrylodan attached to Hsp27 increased 4-5-fold upon interaction with F-actin. Titration of the fluorescence with F-actin yielded a weak binding ...

Interaction of plasma gelsolin with G-actin and F-actin in the presence and absence of calcium ions.

Plasma gelsolin formed a very tight 1:2 complex with G-actin in the presence of Ca2+, but no interaction between gelsolin and G-actin was detected in the presence of excess EGTA. However, the 1:2 complex dissociated into a 1:1 gelsolin:actin complex and monomeric actin when excess EGTA was added. Plasma gelsolin bound tightly to the barbed ends of actin filaments and also severed filaments in t...

Bacterial Actin and Tubulin Homologs in Cell Growth and Division

In contrast to the elaborate cytoskeletal machines harbored by eukaryotic cells, such as mitotic spindles, cytoskeletal structures detectable by typical negative stain electron microscopy are generally absent from bacterial cells. As a result, for decades it was thought that bacteria lacked cytoskeletal machines. Revolutions in genomics and fluorescence microscopy have confirmed the existence n...