FEBS letters, 1998-02, Vol.423 (1), p.93-97
1998
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Details
- Autor(en) / Beteiligte
- Titel
- Characterisation of the effects of mutation of the caldesmon sequence 691glu‐trp‐leu‐thr‐lys‐thr696 to pro‐gly‐his‐tyr‐asn‐asn on caldesmon‐calmodulin interaction
- Ist Teil von
- FEBS letters, 1998-02, Vol.423 (1), p.93-97
- Ort / Verlag
- England
- Erscheinungsjahr
- 1998
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- We have investigated the functional properties of a mutant (Cg1) derived from the C‐terminal 99 amino acids of chicken caldesmon, 658–756 (658C) where the sequence 691glu‐trp‐leu‐thr‐lys‐thr696 is changed to pro‐gly‐his‐tyr‐asn‐asn. Cg1 bound Ca2+‐calmodulin with (1/7)th of the affinity as compared to 658C or whole caldesmon. NMR titrations indicate that the contacts of Ca2+‐calmodulin with the Trp‐722 region of the peptide are retained but that those at the mutated site are lost. Most importantly Ca2+‐calmodulin is not able to reverse the Cg1‐induced inhibition. We conclude that the interaction of calmodulin with this caldesmon sequence is crucial for the reversal of caldesmon inhibition of actin‐tropomyosin activation of myosin ATPase. The results are interpreted in terms of multi‐site attachment of actin and Ca2+‐calmodulin to overlapping sequences in caldesmon domain 4b.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1016/S0014-5793(98)00071-4Titel-ID: cdi_pubmed_primary_9506848
- Format
- –
- Schlagworte
- Actin, Animals, Ca(2+) Mg(2+)-ATPase - antagonists & inhibitors, Ca(2+) Mg(2+)-ATPase - metabolism, Calcium - metabolism, Caldesmon, Calmodulin, Calmodulin - metabolism, Calmodulin-Binding Proteins - genetics, Calmodulin-Binding Proteins - metabolism, Cattle, Chickens, DTT, 1,4-dithio-dl-threitol, EGTA, ethylene glycol-O,O′-bis(2-aminoethyl)-N,N,N′,N′-tetraacetic acid, Enzyme Inhibitors - metabolism, Mutagenesis, Myosins - metabolism, NMR, Nuclear Magnetic Resonance, Biomolecular - methods, PAGE, polyacrylamide gel electrophoresis, Rabbits, Regulation, S-1, chymotryptic myosin subfragment-1, SDS, sodium dodecyl sulphate, Sheep, Smooth muscle, Structure-Activity Relationship, Titrimetry, Tropomyosin, Tryptophan fluorescence