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Literature DB >> 3865205

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

Abstract

The removal of bound metal ions from G-actin uncovered two thiols, Cys-10 and Cys-257. The uncovering of these thiols requires a free calcium concentration lower than 10 nM. Therefore, participation of one or both thiols in Ca2+ binding is suggested. Actin labeled with N-(5-fluoresceinyl)maleimide in the absence of calcium moves as a doublet in NaDodSO4/PAGE. It is suggested that two conformers are induced by metal removal and labeling.

Entities: Chemical

Mesh：

Substances：

Year: 1985 PMID： 3865205 PMCID： PMC390878 DOI： 10.1073/pnas.82.23.7904

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

19 in total

1. Tissue sulfhydryl groups.

Authors: G L ELLMAN
Journal: Arch Biochem Biophys Date: 1959-05 Impact factor: 4.013

2. 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

3. 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

4. The kinetics of the exchange of G-actin-bound 1: N6-ethenoadenosine 5'-triphosphate with ATP as followed by fluorescence.

Authors: F Waechter; J Engel
Journal: Eur J Biochem Date: 1975-09-15

5. Detection of conformational changes in actin by proteolytic digestion: evidence for a new monomeric species.

Authors: S A Rich; J E Estes
Journal: J Mol Biol Date: 1976-07-15 Impact factor: 5.469

6. 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

7. Complete amino-acid sequence of actin of rabbit skeletal muscle.

Authors: M Elzinga; J H Collins; W M Kuehl; R S Adelstein
Journal: Proc Natl Acad Sci U S A Date: 1973-09 Impact factor: 11.205

8. Cyanylation of sulfhydryl groups by 2-nitro-5-thiocyanobenzoic acid. High-yield modification and cleavage of peptides at cysteine residues.

Authors: Y Degani; A Patchornik
Journal: Biochemistry Date: 1974-01-01 Impact factor: 3.162

6. Separating the isomers--efficient synthesis of the N-hydroxysuccinimide esters of 5 and 6-carboxyfluorescein diacetate and 5 and 6-carboxyrhodamine B.

Authors: Aurélie Brunet; Tashfeen Aslam; Mark Bradley
Journal: Bioorg Med Chem Lett Date: 2014-05-04 Impact factor: 2.823

6 in total

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

1. Tissue sulfhydryl groups.

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

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

4. The kinetics of the exchange of G-actin-bound 1: N6-ethenoadenosine 5'-triphosphate with ATP as followed by fluorescence.

5. Detection of conformational changes in actin by proteolytic digestion: evidence for a new monomeric species.

6. 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.

7. Complete amino-acid sequence of actin of rabbit skeletal muscle.

8. Cyanylation of sulfhydryl groups by 2-nitro-5-thiocyanobenzoic acid. High-yield modification and cleavage of peptides at cysteine residues.

9. The exchangeability of actin-bound calcium with various divalent cations.

10. A fluorescent probe for conformational changes in skeletal muscle G-actin.

Review 1. Tightly-bound divalent cation of actin.

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

Review 3. Actin filaments-A target for redox regulation.

Review 4. Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation.

5. Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin.

6. Separating the isomers--efficient synthesis of the N-hydroxysuccinimide esters of 5 and 6-carboxyfluorescein diacetate and 5 and 6-carboxyrhodamine B.