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  The ternary complex of DNase I, actin and thymosin β4

Reichert, A., Heintz, D., Echner, H., Voelter, W. J., & Faulstich, H. (1996). The ternary complex of DNase I, actin and thymosin β4. FEBS Letters, 387(3), 132-136. doi:10.1016/0014-5793(96)00488-7.

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FEBSLett_387_1996_132.pdf (Any fulltext), 486KB
 
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 Creators:
Reichert, Andreas, Author
Heintz, Daniela, Author
Echner, Hartmut, Author
Voelter, Wolfgang J., Author
Faulstich, Heinz1, Author              
Affiliations:
1Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              

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Free keywords: Actin; Thymosin β4; DNase I; Ternary complex; Thiol-specific crosslinking
 Abstract: We have recently described a method for identifying contact sites between actin and thymosin β4 (Tβ4) by following spectrophotometrically the extent and kinetics of distinct, thiolspecific crosslinking reactions between appropriate derivatives of the two proteins [Reichert et al. (1996) J. Biol. Chem. 271, 1301–1308]. In the present study this method was used to show that such crosslinking, which is indicative of complex formation, occurs to the same extent with the actin-DNase I complex as with pure actin, although at a somewhat lower rate. Further evidence for the formation of the ternary complex was given by gel electrophoresis. From fluorescence spectroscopy the K D value of Tβ4 from the actin-DNase I complex was found to be identical to that from pure actin. In line with these data, the capacity of actin for inhibiting DNase I was not affected by the addition of Tβ4. In conclusion, DNase I and Tβ4 are independent of each other in their interaction with actin, suggesting that the binding sites of thymosin β4 and DNase I on actin do not overlap. A ternary complex of DNase I, actin and Tβ4, if obtained in crystalline form, could thus provide an approach for studying the interface of Tβ4 and actin by X-ray analysis.

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Language(s): eng - English
 Dates: 1996-03-111996-04-271999-11-301996-06-03
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665193
DOI: 10.1016/0014-5793(96)00488-7
Other: 6859
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 387 (3) Sequence Number: - Start / End Page: 132 - 136 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501