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Literature DB >> 6374662

Proteolysis and structure of skeletal muscle actin.

Abstract

Under standard conditions, G-actin has been submitted to nine proteases of varying specificity, and in each case the pattern of fragments produced has been studied by NaDodSO4 gel electrophoresis. The results suggest that the actin monomer consists of a large region (ca. 33 kilodaltons) and a small, easily degraded region (ca. 9 kilodaltons). The COOH terminus is in the large region. Consideration of primary sequence homologies, medium resolution maps of actin crystals, and certain reactions of actin suggests that the NH2 terminus is in the small region, as is the negative sequence to which a divalent metal cation is normally chelated, but that the nucleotide-binding site is on the large region near the junction between the regions. From analysis of these results, numerous properties of actin are understandable.

Entities: Chemical

Mesh：

Substances：

Year: 1984 PMID： 6374662 PMCID： PMC345282 DOI： 10.1073/pnas.81.12.3680

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

38 in total

1. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin.

Authors: A G Weeds; R S Taylor
Journal: Nature Date: 1975-09-04 Impact factor: 49.962

2. Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin.

Authors: J H Collins
Journal: Nature Date: 1976-02-26 Impact factor: 49.962

3. Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1.

Authors: R Takashi
Journal: Biochemistry Date: 1979-11-13 Impact factor: 3.162

4. Protein-protein interactions of proteolytic fragments of actin.

Authors: P Johnson; P J Wester; R S Hikida
Journal: Biochim Biophys Acta Date: 1979-05-23

5. ATP binding to a protease-resistant core of actin.

Authors: G R Jacobson; J P Rosenbusch
Journal: Proc Natl Acad Sci U S A Date: 1976-08 Impact factor: 11.205

6. Proteolytic approach to structure and function of actin recognition site in myosin heads.

Authors: D Mornet; R U Bertrand; P Pantel; E Audemard; R Kassab
Journal: Biochemistry Date: 1981-04-14 Impact factor: 3.162

7. Conformational changes of F-actin-epsilon-ADP in thin filaments in myosin-free muscle fibers induced by Ca2+.

Authors: T Yanagida; F Oosawa
Journal: J Mol Biol Date: 1980-06-25 Impact factor: 5.469

8. Anti-actin antibodies of human and rabbit origin.

Authors: A Fagraeus; R Norberg; G Biberfeld
Journal: Ann Immunol (Paris) Date: 1978 Feb-Mar

9. Proton nuclear magnetic resonance and electron paramagnetic resonance studies on skeletal muscle actin indicate that the metal and nucleotide binding sites are separate.

Authors: J A Barden; R Cooke; P E Wright; C G dos Remedios
Journal: Biochemistry Date: 1980-12-09 Impact factor: 3.162

Review 10. Structural aspects of actomyosin interaction.

Authors: R Kassab; D Mornet; P Pantel; R Bertrand; E Audemard
Journal: Biochimie Date: 1981-04 Impact factor: 4.079

18 in total

1. Expression of human beta-myosin heavy chain fragments in Escherichia coli; localization of actin interfaces on cardiac myosin.

Authors: P Eldin; M Le Cunff; K W Diederich; T Jaenicke; B Cornillon; D Mornet; H P Vosberg; J J Léger
Journal: J Muscle Res Cell Motil Date: 1990-10 Impact factor: 2.698

Proteolysis and structure of skeletal muscle actin.

1. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin.

2. Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin.

3. Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1.

4. Protein-protein interactions of proteolytic fragments of actin.

5. ATP binding to a protease-resistant core of actin.

6. Proteolytic approach to structure and function of actin recognition site in myosin heads.

7. Conformational changes of F-actin-epsilon-ADP in thin filaments in myosin-free muscle fibers induced by Ca2+.

8. Anti-actin antibodies of human and rabbit origin.

9. Proton nuclear magnetic resonance and electron paramagnetic resonance studies on skeletal muscle actin indicate that the metal and nucleotide binding sites are separate.

Review 10. Structural aspects of actomyosin interaction.

1. Expression of human beta-myosin heavy chain fragments in Escherichia coli; localization of actin interfaces on cardiac myosin.

2. Chemical evidence for the existence of activated G-actin.

3. The accessibility of the thiol groups on G- and F-actin of rabbit muscle.

4. Effect of self-association on the structural organization of partially folded proteins: inactivated actin.

5. Coupling of nonpolymerizable monomeric actin to the F-actin binding region of the myosin head.

6. Stabilization of a primary loop in myosin subfragment 1 with a fluorescent crosslinker.

7. The enterotoxin of Bacteroides fragilis is a metalloprotease.

8. The interaction of caldesmon with the COOH terminus of actin.

9. Exposure of actin thiols by the removal of tightly held calcium ions.

10. Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions.