Research Profile
Parvulin 14 is peptidyl-prolyl cis/trans isomerase with unknown biological function. The protein is structurally well characterized and was reported to bind to pre-ribosomal ribonucleoprotein particles, and sequence specifically to bent double-stranded DNA. Such bent A/T rich segments of DNA are supposed to dictate nucleosome positioning and play a role in transcription initiation. We intend to elucidate the function of hPar14 as well as its transcriptional regulation. In the projected studies we plan to investigate the Par14 promoter in more detail to find genes that are regulated by Par14 and to elucidate Par14 function in different cell lines with the RNAi technique.

Selected Publications
Mueller, J.W., Kessler, D., Neumann, D., Stratmann, T., Papatheodorou, P., Hartmann-Fatu, C. and Bayer, P. (2006) Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation. BMC Molecular Biology, 7:9.

Bayer, E., Thutewohl, M., Christner, C., Waldmann, H. and Bayer, P. (2005) Identification of a class of hPin1 inhibitors that induce apoptosis in a mammalian Ras cancer cell line. Chem. Commun, 4, 516 - 518.

Reimer, T., Weiwad, M., Schierhorn, A., Ruecknagel, P.-K., Rahfeld, J.-U., Bayer, P. and Fischer, G. (2003) Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14. J.Mol.Biol., 330, 955-966.

Bayer, E., Goettsch, S., Mueller, J.W., Griewel, B., Guiberman, E., Mayr, L.M., and Bayer, P. (2003) Structural analysis of the mitotic regulator hPin1 in solution: Insights into domain architecture and substrate binding. J.Biol.Chem., 278, 26183-26193.

Surmacz, T.A., Bayer, E., Rahfeld, J.U., Fischer, G. and Bayer, P. (2002) The N-terminal domain of hPar14 is necessary for entry to the nucleus and high-affinity DNA-binding. J.Mol.Biol, 321, 235-247.

Sekerina, E. Rahfeld, J.U., Fanghänel, J., Müller, J., Fischer, G., and Bayer, P. (2000): NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hpin1 but indicates a different functionality of the protein. J.Mol.Biol. 301, 1003-1017.