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6 results on '"Birkenmeier O"'

1. The NMR solution structure of the artificial protein M7 matches the computationally designed model

Author

Stordeur, C., Dallüge, R., Birkenmeier, O., Wienk, H.L.J., Rudolph, R., Lange, C., Lücke, C., NMR-spectroscopie, and Dep Scheikunde

Abstract

Rapid progress has been made in the field of protein design over the past couple of years. Computational design algorithms have been used to (i) stabilize naturally occurring proteins,[1][2] (ii) increase the solubility of membrane proteins,[3] and (iii) create de novo proteins that feature previously unknown structural folds.[4] Hence, computational protein design opens a multitude of possibilities to study the complex processes of protein folding and to possibly create new structures with novel functional properties. The first completely de novo designed protein TOP7 (PDB 1QYS), for example, provided the opportunity to explore the energy landscape of a protein structure that was never exposed to natural selection pressure.[5] The long-term goal of this research field is the ability to design proteins that perform the desired functions and exhibit high stability for possible application in industry and therapy.

Published
2008

4. Plakophilin 1 stimulates translation by promoting eIF4A1 activity.

Author

Wolf A, Krause-Gruszczynska M, Birkenmeier O, Ostareck-Lederer A, Hüttelmaier S, and Hatzfeld M

Subjects
Adenosine Triphosphatases metabolism, Cell Line, Cell Proliferation, Cell Size, Humans, Protein Binding, Protein Transport, RNA Cap Analogs metabolism, RNA Caps metabolism, RNA, Small Interfering metabolism, Secretory Vesicles metabolism, Eukaryotic Initiation Factor-4A metabolism, Plakophilins metabolism, Protein Biosynthesis
Abstract

Plakophilins 1-3 (PKP1-3) are desmosomal proteins of the p120(ctn) family of armadillo-related proteins that are essential for organizing the desmosomal plaque. Recent findings identified PKPs in stress granules, suggesting an association with the translational machinery. However, a role of PKPs in controlling translation remained elusive so far. In this study, we show a direct association of PKP1 with the eukaryotic translation initiation factor 4A1 (eIF4A1). PKP1 stimulated eIF4A1-dependent translation via messenger RNA cap and encephalomyocarditis virus internal ribosomal entry site (IRES) structures, whereas eIF4A1-independent translation via hepatitis C virus IRES was not affected. PKP1 copurified with eIF4A1 in the cap complex, and its overexpression stimulated eIF4A1 recruitment into cap-binding complexes. At the molecular level, PKP1 directly promoted eIF4A1 adenosine triphosphatase activity. The stimulation of translation upon PKP1 overexpression correlated with the up-regulation of proliferation and cell size. In conclusion, these findings identify PKP1 as a regulator of translation and proliferation via modulation of eIF4A1 activity and suggest that PKP1 controls cell growth in physiological and pathological conditions.

Published
2010
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6. A tetrapeptide fragment-based design method results in highly stable artificial proteins.

Author

Dallüge R, Oschmann J, Birkenmeier O, Lücke C, Lilie H, Rudolph R, and Lange C

Subjects
Amino Acid Sequence, Computer-Aided Design, Computers, Molecular, Indicators and Reagents, Magnetic Resonance Spectroscopy, Proteins genetics, Proteins isolation & purification, Spectrometry, Fluorescence, Ultracentrifugation, Oligopeptides chemistry, Peptide Fragments chemistry, Proteins chemistry
Abstract

Computational protein design has progressed rapidly over the last years. A number of design methods have been proposed and tested. In this paper, we report the successful application of a fragment-based method for protein design. The method uses statistical information on tetrapeptide backbone conformations. The previously published artificial fold of TOP 7 (Kuhlman et al., Science, 2003; 302:1364-1368) was chosen as template. A series of polypeptide sequences were created that were predicted to fold into this target structure. Two of the designed proteins, M5 and M7, were expressed and characterized by fluorescence spectroscopy, circular dichroism and NMR. They showed the hallmarks of well-ordered tertiary structure as well as cooperative folding/unfolding transitions. Furthermore, the two novel proteins were found to be highly stable against temperature and denaturant-induced unfolding., (2007 Wiley-Liss, Inc.)

Published
2007
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