Biochemical properties of cofilin

Range Table - link
Organism Fission yeast Schizosaccharomyces pombe
Reference Chen Q, Pollard TD. Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring. J Cell Biol. 2011 Oct 31 195(3):485-98. doi: 10.1083/jcb.201103067. p.488 table IIPubMed ID22024167
Method "[Researchers] tested the hypothesis that the role of cofilin in cytokinesis is to sever actin filaments during assembly of contractile rings. [Their] initial observations of the temperature-sensitive cofilin adf1-1 strain by fluorescence microscopy of live cells showed that precursors called nodes failed to condense into a contractile ring at the restrictive temperature. The adf1-1 cofilin protein (L57S) was not sufficiently stable to purify, so [they] created seven new mutations based on temperature-sensitive mutations of budding yeast cofilin (Lappalainen et al., 1997)."
Comments "[Researchers] characterized the biochemical properties of cofilin-M2 and cofilin-M3 purified from bacteria (Fig. S2 A). Cofilin-M3 is slightly more stable to urea denaturation than the wild-type protein, whereas cofilin-M2 is slightly less stable (Table II Fig. S2 B)." See notes beneath table
Entered by Uri M
ID 111103