Sabine Rech

Sabine Rech

Director of the Master of Biotechnology Program

Duncan Hall, Room 644
Telephone: (408) 924-4832
FAX: (408) 924-4840
E-mail: srech@email.sjsu.edu

 

Education

University of Santa Clara B.S. 1984 Biology
San Jose State University M.A. 1987 Microbiology
UC Davis Ph.D. 1992 Microbiology
UCLA Postdoc 1998-1999 Micro and Mol Gen
Michigan State University / Center for Microb. Ecology Postdoc 1998-1999 Env. Microbiol.

 

Courses Taught

Micro 101 - General Microbiology
Micro 122 - Bacterial Diversity
Micro 127 - Microbial Physiology
Biol 255M - Seminar in Advanced Biology - M & M

 

Research Interests

My research interests lie in the area of environmental microbiology and microbial diversity. Currently my laboratory is involved in two active research projects. The first project focuses on the isolation of bromination enzymes from bacteria in marine or high salt environments. We have isolated microorganisms capable of brominating organics from a salt evaporation pond as well as the slime of a marine invertebrate worm classified as an acorn worm. Our studies involve the identification of the bacteria by isolating and sequencing their 16SrRNA genes as well as the isolation and characterization of the bromination enzymes, which include bromoperoxidases. The second project focuses on the investigation of the microbial diversity in the soil of salt marshes in the process of natural restoration as well as the role of the denitrifying organisms in this process. We are using restriction fragment length polymorphism (RFLP) to begin to understand the diversity throughout the growing season. This technique involves the extraction of the total community DNA from the soil followed by the amplification of the bacterial 16SrRNA genes. The amplified genes are grouped into operational taxonomic units (OTUs) by restriction digests and representatives are sequenced. We are examining three marshes, which are in various restoration stages ranging from a mud flat to an almost completely restored wetland. Both projects require the isolation and quantification of DNA and protein using a highly sensitive method. This research will be greatly supported by the grant of fluorometer from Turner BioSystems.

 

Selected Publications

1. Komives, C., S. Rech and M. Mc. Neil. 2004. Laboratory Experiment on Gene Subcloning For Chemical Engineering Students. Chemical Engineering Education 38: 212-215

2. Boothby, J. T., R. Miller, S. Rech and R. Hicks. 2004 Teaching Phagocytosis using Flow Cytometry. Microbiological Education 5:36-41

3. McNicholas PM, M. Mazzotta, S. A. Rech and R. P. Gunsalus. 1998. Functional dissection of the molybdate-responsive transcription regulator, ModE, from Escherichia coli. J. Bacteriol. 180:4638-4643.

4. Hu, Yonglin, S. Rech, R.P. Gunsalus and CO C. Rees. 1997. Crystal Structure of ModA, a molybdate transport protein, complexed with molybdate and tungstate. Nature Structural Biology 4:703-707.

5. Schroeder, Imke, S. Rech, T. Krafft and J. Macy. 1997. Purification and characterization of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272:23765-23768.

6. Mc Nicholas, Paul M., S. Rech and R. Gunsalus. 1997. Characterization of the ModE DNA binding sites in the control regions of modABCD and moaABCDE of Escherichia coli. J. Mol. Micro. 23:515-524.

7. Rech, Sabine, C. Wolin and R. Gunsalus. 1996. Properties of the Periplasmic ModA Molybdate-Binding Protein of Escherichia coli. J. Biol. Chem. 271:2557-2562.

8. Rech, Sabine, U. Deppenmeier and R. Gunsalus. 1995. Regulation of the Molybdate Transport Operon, modABCD, of Escherichia coli in Response to Molybdate Availability. J. Bacteriol. 177:1023-1029.

9. Rech, Sabine and J. Macy. 1992. The Terminal Reductases for Selenate and Nitrate Respiration in Thauera selenatis are two Distinct Enzymes. J. Bacteriol. 174:7316-7320.

10. Macy, J. M., S. Rech, G. Auling, M. Dorsch, E. Stackebrandt and L. I. Sly. 1993. Thauera selenatis gen. nov., sp. nov., a Member of the Beta Subclass of Proteobacteria with a Novel type of Anaerobic Respiration. Int. J. Sys. Bacteriol. 43:135-142.