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  Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine

Batra, R., & Manstein, D. J. (1999). Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine. Biological Chemistry, 380(7), 1017-1023. doi:10.1515/BC.1999.126.

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Genre: Zeitschriftenartikel
Alternativer Titel : Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine

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BiologChem_380_1999_1017.pdf (beliebiger Volltext), 651KB
 
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 Urheber:
Batra, Renu1, Autor           
Manstein, Dietmar J.1, Autor           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Schlagwörter: Fluorescence / Molecular motor / Myosin ATPase / Protein engineering
 Zusammenfassung: We created a Dictyostelium discoideum myosin II mutant in which the highly conserved residue Trp-501 was replaced by a tyrosine residue. The mutant myosin alone, when expressed in a Dictyostelium strain lacking the functional myosin II heavy chain gene, supported cytokinesis and multicellular development, processes which require a functional myosin in Dictyostelium. Additionally, we expressed the W501 Y mutant in the soluble myosin head fragment M761-2R (W501Y-2R) to characterise the kinetic properties of the mutant myosin motor domain. The affinity of the mutant myosin for actin was approximately 6-fold decreased, but other kinetic properties of the protein were changed less than 2-fold by the W501Y mutation. Based on spectroscopic studies and structural considerations, Trp-501, corresponding to Trp-510 in chicken fast skeletal muscle myosin, has been proposed to be the primary ATP-sensitive tryptophanyl residue. Our results confirm these conclusions. While the wild-type construct displayed a 10% fluorescence increase, addition of ATP to W501Y-2R was not followed by an increase in tryptophan fluorescence emission

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Sprache(n): eng - English
 Datum: 1999-04-281999-06-111999-07
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Art des Abschluß: -

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Titel: Biological Chemistry
  Andere : Biological Chemistry Hoppe-Seyler (Berlin)
  Kurztitel : Biol Chem Hoppe Seyler
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: Berlin : W. de Gruyter
Seiten: - Band / Heft: 380 (7) Artikelnummer: - Start- / Endseite: 1017 - 1023 Identifikator: Anderer: 1437-4315
ISSN: 1431-6730
CoNE: https://pure.mpg.de/cone/journals/resource/954927622123