Fernando Gonzalez, Ph.D.

Associate Professor


Midwestern University
AZCOM
Department of Microbiology and Immunology
Agave Hall, 217G
19555 N. 59th Avenue
Glendale, AZ 85308

Office: (623) 572-3723
Contact

EDUCATION

Ph. D. Biochemistry and Molecular Biology University of Texas Southwestern Medical Center
M.S. Molecular Biology  University of Texas at El Paso
B.S. Microbiology University of Texas at El Paso

RESEARCH SUMMARY

Candida species are the causative organisms for the majority of all fungal infections in the United States, including 86% of all nosocomial fungal infections.  In severely ill patients, it is estimated that candidemia results in the burden of 30 days excess hospital stay and 40% mortality.  Additionally, overgrowth of Candida albicans is responsible for the majority of Candida infections.  Virulence in C. albicans is thought to be enhanced following transition of the organism from budding yeast to mold. During the budding yeast-to-hyphae transition (BHT), it is known that a signal transduction pathway leads to the production of hyphae-specific proteins, including a family of secreted aspartyl protease (SAP) proteins. While it is generally accepted that increased SAP protein expression is responsible for an increase in virulence of Candida, knowledge regarding the role of intracellular proteolysis on fungal virulence is largely undiscovered.  Without such knowledge, regulatory mechanisms of opportunistic fungal pathogen virulence cannot truly be understood. Using a collection of biochemical and molecular biological techniques, our lab is currently investigating the role of regulated proteolysis in fungal pathogenesis.

SELECTED PUBLICATIONS

The Lap3p aminopeptidase is not  solely responsible for bleomycin resistance in Candida albicans.  Rogers AR,  Graves SM, and Gonzalez F. Journal of Yeast and Fungal Research (2014) 5(3):39-49.  

Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo.
Archer CT, Delahodde A, Gonzalez FJohnston SA, Kodadek T.J Biol Chem. 2008 May 2;283(18):12614-23. doi: 10.1074/jbc.M801050200. Epub 2008 Mar 6.
PMID: 18326036

Physical and functional association of RNA polymerase II and the proteasome.
Gillette TG, Gonzalez F, Delahodde A, Johnston SA, Kodadek T.Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5904-9. Epub 2004 Apr 6.
PMID: 15069196

Recruitment of a 19S proteasome subcomplex to an activated promoter.
Gonzalez F, Delahodde A, Kodadek T, Johnston SA.Science. 2002 Apr 19;296(5567):
PMID: 11964484

Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases.
Russell SJ, Gonzalez F, Joshua-Tor L, Johnston SA. Chem Biol. 2001 Oct;8(10):941-50. PMID: 11590019

The Gal4 activation domain binds Sug2 protein, a proteasome component, in vivo and in vitro.
Chang C, Gonzalez F, Rothermel B, Sun L, Johnston SA, Kodadek T.J Biol Chem. 2001 Aug 17;276(33):30956-63. Epub 2001 Jun 19.
PMID: 11418596

The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II.
Ferdous A, Gonzalez F, Sun L, Kodadek T, Johnston SA.Mol Cell. 2001 May;7(5):981-91. PMID: 11389845

Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease.
O'Farrell PA, Gonzalez F, Zheng W, Johnston SA, Joshua-Tor L.Structure. 1999 Jun 15;7(6):619-27. PMID: 10404591