Vordiplom, Universität of Münster, Germany, 1988
Ph.D. UMass, Amherst, 1994
Postdoc. Harvard Medical School, 1994-1998
Figure 1. Subcellular localization of secreted proteins. Upon secretion and signal peptide processing, Sec and Tat substrates can be released into the extracellular milieu (1), be embedded into the cytoplasmic membrane (CM) via a lipid anchor (2) or a C-terminal transmembrane segment (3). In silico data also suggest that some Sec substrates are anchored to the cell wall (CW) (4) and a number of type IV pilin-like proteins have been shown to assemble into cell appendages (5).
In recent years, we have also focused on characterizing the diversity of Sec and Tat substrates, including substrate functions and subcellular localization. We have identified and confirmed, experimentally, substrate sequences targeted for post-translational modifications, and determined some of the components involved in these modifications. Our in vivo analyses generated information that has allowed us to develop novel subcellular localization prediction programs, as well as improve existing ones, and has led to the identification of novel Hfx. volcanii protein transport components. Further evaluation of combined in vivo and in silico data revealed intriguing patterns suggesting that evolutionary pressures may have determined the use of a specific transport pathway and surface anchoring mechanisms for some substrates.