Abstract:
:The regulatory system of smooth muscle thin filaments is thought to involve a major calcium-calmodulin and actin binding protein: caldesmon. A dissective approach was used to isolate a 35 kDa C-terminal fragment of the molecule and to produce antibodies reacting against both the intact and the 15 kDa N-terminal end of this parental fragment. While this purified 15 kDa caldesmon fragment demonstrates a weak actin association, we observed that it cross-links actin filaments into loose bundles. These structures were labelled with a selective antibody and showed regular periodic striation with repeats of approximately 40 nm. This work brings additional information to previous reports using an actin and calmodulin binding 25 kDa C-terminal fragment of the caldesmon molecule [(1989) J. Biol. Chem. 264, 2869-2875]. We demonstrate that a purified fragment corresponding to a sequence smaller than 96 amino acids, which contains no cystein residue, is able to interact with actin at a single site which is not the calmodulin modulated.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Harricane MC,Cavadore C,Audemard E,Mornet Ddoi
10.1016/0014-5793(90)81150-msubject
Has Abstractpub_date
1990-08-20 00:00:00pages
185-8issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(90)81150-Mjournal_volume
269pub_type
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