Jachen A. Solinger
1995 - Lic. phil. nat. (Diploma) General Microbiology - University of Bern (Switzerland)
1998 - Ph.D. General Microbiology - University of Bern (Switzerland)

e-Mail address: jasolinger@bluewin.ch
The magnificent Rad-Rooster (a science comic)

Positions and experience:
1990-1993 - Diploma studies, Institute of General Microbiology,
University of Bern (Switzerland)
1993-1995 - Diploma research project, Institute of General Microbiology,
University of Bern (Switzerland) with Dr. W.-D. Heyer
1995-1998 - Ph.D. research project, Institute of General Microbiology,
University of Bern (Switzerland) with Dr. W.-D. Heyer
1998-2003 - Post-Doctoral Fellow, Section of Microbiology,
University of California, Davis (USA)

Publications:
Solinger, J.A., Kiianitsa, K., and Heyer, W.-D. (2002)
Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles
Rad51:dsDNA filaments. Mol Cell.10, 1175-1188. [PDF file]
Kiianitsa, K., Solinger, J.A., Heyer, W.-D. (2002)
Rad54 protein exerts diverse modes of ATPase activity on duplex DNA partially
and fully covered with Rad51 protein. J Biol Chem. 277, 46205-46215.[PDF file]
Kim, P.M., Paffett, K.S., Solinger, J.A., Heyer, W.-D., and Nickoloff, J.A. (2002)
Spontaneous and double-strand break-induced recombination, and gene conversion tract lengths,
are differentially affected by overexpression of wild-type or ATPase-defective yeast Rad54.
Nucleic Acids Res. 30, 2727-2735. [PDF
file]
Solinger, J.A. and Heyer, W.-D. (2001) Rad54 protein stimulates the postsynaptic
phase of Rad51 protein-mediated DNA strand exchange.
Proc. Natl. Acad. Sci. USA. 98(15):8447-8453. [PDF file]
Solinger, J.A., Lutz, G., Sugiyama, T., Kowalczykowski, S.C., and Heyer, W.-D. (2001)
Rad54 protein stimulates heteroduplex DNA formation in the synaptic phase of DNA
strand exchange via specific interactions with the presynaptic Rad51 nucleoprotein filament.
J. Mol. Biol. 307(5):1207-1221. [PDF
file]
Mazin, A., Bornarth, C.J., Solinger, J.A., Heyer, W.-D., and Kowalczykowski, S.C.
(2000) Rad54 protein is targeted to pairing loci by the Rad51 nucleoprotein filament.
Mol. Cell 6, 583-592. [PDF file]
Solinger, J. A., Pascolini, D., and Heyer, W.-D. (1999) Separation-of-function
mutations in the active site of the Saccharomyces cerevisiae
Xrn1p exoribonuclease
reveal a specific role in meiosis. Mol. Cell. Biol. 19, 5930-5942.
[PDF file]
Bashkirov, V. I., Scherthan, H., Solinger, J. A., Buerstedde, J.-M., and Heyer, W.-D.
(1997) A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4
tetraplex substrates. J. Cell. Biol. 136, 761-773. [PDF
file]
Holler, A., Bashkirov, V. I., Solinger, J. A., Reinhart, U., and Heyer, W.-D. (1995)
Use of monoclonal antibodies in the functional characterization of the
Saccharomyces cerevisiae Sep1 protein. Eur. J. Biochem. 231, 329-336.
Bashkirov, V. I., Solinger, J. A., and Heyer, W.-D. (1995) Structure-function analysis
in the multi-functional SEP1 gene (=KEM1, XRN1) encoding a protein required for
the transition through meiotic prophase in Saccharomyces cerevisiae. Chromosoma
104, 215-222.