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 |