Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin.

Literature DB >> 2143196

Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin.

D H Schwyter¹, S J Kron, Y Y Toyoshima, J A Spudich, E Reisler.

Abstract

Subtilisin cleaved actin was shown to retain several properties of intact actin including the binding of heavy meromyosin (HMM), the dissociation from HMM by ATP, and the activation of HMM ATPase activity. Similar Vmax but different Km values were obtained for acto-HMM ATPase with the cleaved and intact actins. The ATPase activity of HMM stimulated by copolymers of intact and cleaved actin showed a linear dependence on the fraction of intact actin in the copolymer. The most important difference between the intact and cleaved actin was observed in an in vitro motility assay for actin sliding movement over an HMM coated surface. Only 30% of the cleaved actin filaments appeared mobile in this assay and moreover, the velocity of the mobile filaments was approximately 30% that of intact actin filaments. These results suggest that the motility of actin filaments can be uncoupled from the activation of myosin ATPase activity and is dependent on the structural integrity of actin and perhaps, dynamic changes in the actin molecule.

Entities: Chemical Gene

Mesh：

Substances：

Year: 1990 PMID： 2143196 PMCID： PMC2116201 DOI： 10.1083/jcb.111.2.465

Source DB: PubMed Journal: J Cell Biol ISSN： 0021-9525 Impact factor: 10.539

37 in total

1. Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range.

Authors: D D Thomas; J C Seidel; J Gergely
Journal: J Mol Biol Date: 1979-08-15 Impact factor: 5.469

2. On the origin of the contractile force in skeletal muscle.

Authors: W F Harrington
Journal: Proc Natl Acad Sci U S A Date: 1979-10 Impact factor: 11.205

3. Polarized fluorescence from epsilon-ADP incorporated into F-actin in a myosin-free single fiber: conformation of F-actin and changes induced in it by heavy meromyosin.

Authors: T Yanagida; F Oosawa
Journal: J Mol Biol Date: 1978-12-15 Impact factor: 5.469

4. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility.

Authors: A G Weeds; B Pope
Journal: J Mol Biol Date: 1977-04 Impact factor: 5.469

5. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.

Authors: J A Spudich; S Watt
Journal: J Biol Chem Date: 1971-08-10 Impact factor: 5.157

10. F-actin structure destabilization and DNase I binding loop: fluctuations mutational cross-linking and electron microscopy analysis of loop states and effects on F-actin.

Authors: Zeynep A Oztug Durer; Karthikeyan Diraviyam; David Sept; Dmitri S Kudryashov; Emil Reisler
Journal: J Mol Biol Date: 2009-11-06 Impact factor: 5.469

Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin.

1. Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range.

2. On the origin of the contractile force in skeletal muscle.

3. Polarized fluorescence from epsilon-ADP incorporated into F-actin in a myosin-free single fiber: conformation of F-actin and changes induced in it by heavy meromyosin.

4. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility.

5. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.

6. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

7. Conformational change and cooperativity in actin filaments free of tropomyosin.

8. Myosin minifilaments.

9. Dynamic study of F-actin by quasielastic scattering of laser light.

10. Cross-linking of the skeletal myosin subfragment 1 heavy chain to the N-terminal actin segment of residues 40-113.

1. Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.

2. F-actin retains a memory of angular order.

Review 3. Actin and the smooth muscle regulatory proteins: a structural perspective.

4. Actin as the generator of tension during muscle contraction.

5. Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization.

6. Muscle contraction and in vitro movement: role of actin?

7. Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N terminus.

8. Mutation of actin Tyr-53 alters the conformations of the DNase I-binding loop and the nucleotide-binding cleft.

9. Inhibition of actin filament movement by monoclonal antibodies against the motor domain of myosin.

10. F-actin structure destabilization and DNase I binding loop: fluctuations mutational cross-linking and electron microscopy analysis of loop states and effects on F-actin.