Donna Gordon

Donna Gordon

Division

  • Faculty

Classification

  • Professor

Discipline

  • Physiological, Cellular and Developmental Biology
  • Microbiology and Molecular Biology

Contact

gordon@biology.msstate.edu
662-325-9337

Address

  • 222 Harned Hall
  • B.S. Biology/Genetics, Pennsylvania State Univ.
  • Ph.D. Cell & Molecular Biology, University of Pennsylvania School of Medicine
  • University of Pennsylvania
  • University of Medicine and Dentistry of New Jersey

From yeast to humans, mitochondria form a dynamic interconnected network that provides an efficient system to transfer energy between different areas of the cell. The number and morphology of mitochondria within a cell are controlled by precisely regulated rates of organelle fusion and fission. Mitochondrial fusion is a complex process involving the joining of both the outer and inner membranes of two adjacent mitochondria in a highly coordinated and accurate manner. Perturbations in fusion result in mitochondrial fragmentation, loss of mitochondrial DNA, defects in mitochondrial membrane potential and respiration, and poor growth. In the budding yeast, Saccharomyces cerevisiae, a number of proteins have been identified for their role in the maintenance of "normal" mitochondrial morphology. Our work focuses on Pcp1p, a mitochondrial peptidase shown to be involved in the proteolytic processing of the mitochondrial "fusion" protein Mgm1p. Little is known about the molecular mechanism of Pcp1p mediated proteolytic cleavage or the identity of additional Pcp1p substrate proteins. Using genetic, biochemical and cell biological approaches the lab aims to elucidate the role of the Pcp1p protease in mitochondrial dynamics and functions.

Unlu, E., Gordon, D.M., and Telli, M. (2015)  Small RNA sequencing based identificaton of miRNAs in Daphnia magnaPLOS ONE 10(9): e0137617. DOI: 10.1371/journal.pone.0137617.

Pandley, A., Gordon D.M.,  Pain, J., Stemmler, T.L., Dancis, A. and Pain, D. (2013)  Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding Sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly.  The Journal of Biological Chemistry 288(52): 36773-36786.  DOI: 10.1074/jbc.P113.525857.

Unlu, E., Narayanan, N. and Gordon, D.M.  (2013) Characterization of fungal RTG2 genes in retrograde signaling of Saccharomyces cerevisiaeFEMS Yeast Research 13(5): 495-503.  DOI: 10.1111/1567-1364.12055.

Emrick, D., Ravichandran, A., Gosai, J., Lu, S., Gordon, D.M., and Smith, L. (2013)  The antifungal occidiofungin triggers an apoptotic mechanism of cell death in yeast.  Journal of Natural Products 76(5): 829-838.  doi: 10.1021/np300678e.

Ellis, D., Gosai, J., Emrick, C., Heintz, R., Romans, L., Gordon, D., Lu, S-E, and Smith, L. (2012) Occidiofungin's chemical stability and in vitro potency against Candida species.  Antimicrobial Agents and Chemotherapy 56(2): 765-9. DOI: 10.1128/AAC.05231-11.