| Autor: |
Vikhorev PG; Institute of Cytology RAS, St. Petersburg., Avrova SV, Ermakov VS, Copeland O, Marston SB, Borovikov IuS |
| Jazyk: |
ruština |
| Zdroj: |
Tsitologiia [Tsitologiia] 2000; Vol. 42 (11), pp. 1069-74. |
| Abstrakt: |
TRITC-phalloidin or FITC-labeled F-actin of ghost muscle fibers was bound to tropomyosin and C-terminal recombinant fragments of caldesmon CaDH1 (residues 506-793) or CaDH2 (residues 683-767). After that the fibers were decorated with myosin subfragment 1. In the absence of caldesmon fragments, subfragment 1 interaction with F-actin caused changes in parameters of polarized fluorescence, that were typical of "strong" binding of myosin heads to F-actin and of the "switched on" conformational state of actin. CaDH1 inhibited, whereas CaDH2 activated the effect of subfragment 1. It is suggested that C-terminal part of caldesmon may modulate the transition of F-actin subunits from the "switched on" to the "switched off" state. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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