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  Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity

Schrimpf, A., Hempel, F., Li, A., Linne, U., Maier, U. G., Reetz, M. T., et al. (2018). Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity. Biochemistry, 57(26), 3658-3664. doi:10.1021/acs.biochem.8b00475.

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 Creators:
Schrimpf, Andreas1, Author
Hempel, Franziska2, Author
Li, Aitao1, 3, Author              
Linne, Uwe1, Author
Maier, Uwe G.2, 4, Author
Reetz, Manfred T.1, 3, Author              
Geyer, Armin1, Author
Affiliations:
1Department of Chemistry, Philipps-Universität Marburg, Hans-Meerwein-Straße 4, 35032 Marburg, Germany, ou_persistent22              
2Department of Biology, Philipps-Universität Marburg, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany, ou_persistent22              
3Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445588              
4 LOEWE Zentrum für Synthetische Mikrobiologie (SYNMIKRO), Hans-Meerwein-Straße 6, D-35032 Marburg, Germany, ou_persistent22              

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 Abstract: Dimeric disulfide-linked peptides are formed by the regioselective oxidative folding of thiol precursors containing the CX3CX2CX3C tetracysteine motif. Here, we investigate the general applicability of this peptide as a dimerization motif for different proteins. By recombinant DNA technology, the peptide CHWECRGCRLVC was loaded with proteins, and functional homodimers were obtained upon oxidative folding. Attached to the N-terminus of the dodecapeptide, the prokaryotic enzyme limonene epoxide hydrolase (LEH) completely forms a covalent antiparallel dimer. In a diatom expression system, the monoclonal antibody CL4 mAb is released in its functional form when its natural CPPC central parallel hinge is exchanged for the designed tetra-Cys hinge motif. To improve our understanding of the regioselectivity of tetra-disulfide formation, we provoked the formation of heterodimeric hinge peptides by mixing two different tetra-Cys peptides and characterizing the heterodimer by mass spectrometry and nuclear magnetic resonance spectroscopy.

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Language(s): eng - English
 Dates: 2018-05-032018-06-042018-07-03
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.biochem.8b00475
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 57 (26) Sequence Number: - Start / End Page: 3658 - 3664 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103