Premium
Calponin binds G‐actin and F‐actin with similar affinity
Author(s) -
Ferjani Imen,
Fattoum Abdellatif,
Maciver Sutherland K.,
Manai Mohamed,
Benyamin Yves,
Roustan Claude
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.065
Subject(s) - calponin , actin , actin binding protein , förster resonance energy transfer , chemistry , actina , cytoplasm , biophysics , microbiology and biotechnology , biochemistry , actin cytoskeleton , cytoskeleton , biology , fluorescence , cell , physics , quantum mechanics
Calponins are actin‐binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F‐actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affinity ( K d of 0.15 μM). We show that the arrangement of binding is similar to that of F‐actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29 Å when measured by fluorescent resonance energy transfer, the same distance as previously reported for F‐actin.