RNA Protein Interaction

Research areas:

The group is involved in three different projects. One of these focuses on the posttranslational modification of the model G-protein EF-Tu (elongation factor Tu). The phosphorylation of the prokaryotic protein was discovered; it seems to be an essential step in protein biosynthesis.

The second field of interest is the structural analysis of the 5S rRNA and its subdomains.

The major topic of the group is the investigation of the structure and function of the eukaryotic H19 RNA, which is expressed during embryogenesis and in various tumours. The function of this mRNA-like molecule is unknown.

Selected publications:

Lippmann C., Lindschau C., Vijgenboom E., Schröder W., Bosch L. & Erdmann V.A. (1993) Prokaryotic elongation factor is phosphorylated in vivo. J.Biol.Chem., 268, 601-607

Alexander C., Mesters J.R., Kraal B., Bilgin N., Hilgenfeld R., Lindschau C., Erdmann V.A. & Lippmann C. (1995) Phosphorylation of EF-Tu prevents ternary complex formation. J.Biol.Chem. 270, 14541-14547

Polekhina G., Thirup S., Kjeldgaard M., Nissen P., Lippmann C. & Nyborg J. (1996) Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure, 15, 1141-1151

Kraal B, Lippmann C, Kleanthous C. (1999) Translational regulation by modifications of the elongation factor Tu. Folia Microbiol, 44 (2), 131-41. Review.

Lorenz S, Perbandt M, Lippmann C, Moore K, DeLucas LJ, Betzel C, Erdmann VA. (2000) Crystallization of engineered Thermus flavus 5S rRNA under earth and microgravity conditions. Acta Crystallogr D Biol Crystallogr., 56 (Pt 4), 498-500

Perbandt M, Vallazza M, Lippmann C, Betzel Ch, Erdmann VA. (2001) Structure of an RNA duplex with an unusual G·C in wobble-like conformation at 1.6 resolution. Acta Crystallogr D Biol Crystallogr., 57 (Pt 4), 219-224

Last update: 29.1.2001