Paul Berg

    Email: pberg@cmgm.stanford.edu

Web: No lab page.

A dominant theme of research in my laboratory during the past ten years has been the development and application of recombinant DNA and related methodologies for the analysis of genetic recombination in eukaryotic cells.

An important goal in cell and molecular genetics of mammalian cells is to be able to target exogenous genes to specific loci in the genome. This has been achieved although the frequency is low. Our current program aims to discover more about the process of gene conversion, a non-reciprocal recombination process in which sequences from one duplex DNA replace a corresponding region in a homologous duplex DNA. Both in vitro and in vivo experiments are being pursued to explore this reaction, particularly the isolation of yeast mutants blocked in their ability to carry out gene conversion between episomal and chromosomal homologous sequences. We are exploring this strategy for targeting alterations in chromosomal genes of embryonic stem cells with a goal of creating mutant animals.

The HIV-1 virus induces an immunodeficiency disease in patients it infects by depleting the T-helper population. We are exploring the signal transduction pathway from the T cell receptor as a possible target for the action of one of the viral genes.


Jessberger, R. and Berg, P. (1991) Repair of deletions and double-strand gaps by homologous recombination in a mammalian in vitro system. Mol Cell Biol 11,(1): 445-457. (Medline)

Jessberger, R., Podust, V., Hübscher, U. and Berg, P. (1993) A mammalian protein complex that repairs double-strand breaks and deletions by recombination. J Biol Chem 268, (20): 15070-15079. (Medline)

Firmenich, A. A., Elias-Arnanz, M., and Berg, P. (1995). A novel allele of Saccharomyces cerevisiae RFA1 that is deficient in recombination and repair and suppressible by RAD52. Mol Cell Biol 15, 1620-31. (Medline)

Hays, S. L., Firmenich, A. A., and Berg, P. (1995). Complex formation in yeast double-strand break repair: participation of Rad51, Rad52, Rad55, and Rad57 proteins. Proc Natl Acad Sci U S A 92, 6925-9. (Medline)