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Peptide competition of actin activation of myosin-subfragment 1 ATPase by an amino terminal actin fragment
- Source :
- FEBS Letters. 294:31-34
- Publication Year :
- 1991
- Publisher :
- Wiley, 1991.
-
Abstract
- The amino-terminal region of actin participates in the binding of myosin subfragment 1 (S1) during cross-bridge cycling, thereby assisting in the activation of the magnesium-dependent myosin ATPase. Effects of three actin fragments on the magnesium-dependent S1 and acto-S1 ATPase activities in solution were studied. One of the peptides, containing residues actin 1–44, mimicked the S1 ATPase-activating properties of actin and in turn inhibited acto-S1 ATPase both in a concentration-dependent manner. This suggests peptide competition for the actin binding site on myosin. The other fragments, residues actin 1–18 and 82–119, respectively, had no detectable effect on S1- and acto-S1 ATPase activity.
- Subjects :
- Myosin ATPase
Biophysics
Arp2/3 complex
macromolecular substances
Myosins
Biology
Microfilament
Biochemistry
Structural Biology
Myosin
Genetics
Animals
Cyanogen Bromide
Actin-binding protein
Molecular Biology
Actin
Muscles
Myosin Subfragments
Actin peptide
Actin remodeling
Cell Biology
Actins
Peptide Fragments
Acto-S1-ATPase
Enzyme Activation
Kinetics
Spectrometry, Fluorescence
Profilin
biology.protein
Ca(2+) Mg(2+)-ATPase
Rabbits
S1-ATPase
MDia1
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 294
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....d0fd81ec50d5d6662bfeabfe5ad280a3