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Literature DB >> 1278154

The selective blocking of the polymerization reaction of striated muscle actin leading to a derivative suitable for crystallization. Modification of Tyr-53 by 5-diazonium-(1H)tetrazole.

N Bender, H Fasold, A Kenmoku, G Middelhoff, K E Volk.

Abstract

The polymerization reaction of rabbit muscle actin was completely inhibited by reaction of one amino acid side chain per protein monomer with 5-diazonium-(1H)[14C]tetrazole. A tryptic peptide fingerprint showed a single peptide labeled by the reagent. The peptide was isolated and the labeled amino acid identified by amino acid analysis as Tyr-53. This side chain is not accessible to the reagent in F-actin. The modification is compared to similar inhibitions by other reagents.

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Year: 1976 PMID： 1278154 DOI： 10.1111/j.1432-1033.1976.tb10290.x

Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956

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Cited

10 in total

Review 1. Structure of actin observed by fluorescence resonance energy transfer spectroscopy.

Authors: M Miki; S I O'Donoghue; C G Dos Remedios
Journal: J Muscle Res Cell Motil Date: 1992-04 Impact factor: 2.698

2. Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments.

Authors: Xiong Liu; Shi Shu; Myoung-Soon S Hong; Rodney L Levine; Edward D Korn
Journal: Proc Natl Acad Sci U S A Date: 2006-08-30 Impact factor: 11.205

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

Authors: D F Liu; D Wang; A Stracher
Journal: Biochem J Date: 1990-03-01 Impact factor: 3.857

4. Artificial dimers of native actin: preparation and properties in biological functions.

Authors: H G Bäumert; A Kenmoku; G Middelhoff; F Ortanderl; A Thrun; H Faulstich; W Schiebler; H Fasold
Journal: J Protein Chem Date: 1988-10

5. Studies on the antigenic sites of actin: a comparative study of the immunogenic crossreactivity of invertebrate actins.

Authors: H G De Couet
Journal: J Muscle Res Cell Motil Date: 1983-08 Impact factor: 2.698

6. Unconcerted conformational changes in Arp2/3 complex integrate multiple activating signals to assemble functional actin networks.

Authors: Heidy Y Narvaez-Ortiz; Brad J Nolen
Journal: Curr Biol Date: 2022-01-31 Impact factor: 10.834

The selective blocking of the polymerization reaction of striated muscle actin leading to a derivative suitable for crystallization. Modification of Tyr-53 by 5-diazonium-(1H)tetrazole.

Review 1. Structure of actin observed by fluorescence resonance energy transfer spectroscopy.

2. Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments.

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

4. Artificial dimers of native actin: preparation and properties in biological functions.

5. Studies on the antigenic sites of actin: a comparative study of the immunogenic crossreactivity of invertebrate actins.

6. Unconcerted conformational changes in Arp2/3 complex integrate multiple activating signals to assemble functional actin networks.

Review 7. The polymerization reaction of muscle actin.

Review 8. Post-translational modification and regulation of actin.

9. Probing actin polymerization by intermolecular cross-linking.

10. How actin binds and assembles onto plasma membranes from Dictyostelium discoideum.