ABOUT ME

I was born in the island of Jamaica and grew up in the town of Savanna-La-Mar in the parish of Westmoreland. I came to the United States at the age of 14 and completed High School at Salesian High in New Rochelle, NY. I recieved a B.S. in Biology from Virginia Union University (VUU) in 2000. I fell in love with Science as an undergraduate student researcher in the laboratory of Dr. Anthony Madu at VUU where I performed research aiming at identifying pathogenic bacteria from farm produce. I then enrolled in the Graduate Program at Rutgers University where I completed my doctorate in the department of Plant Biology and Pathology in 2006 under the direction of Dr. Thomas Leustek. I joined the faculty in the School of Life Sciences in the Fall of 2008 following a post-doctoral fellowship at Rutgers Univeristy. I currenlty live in Hilton, NY with my wife Candice and my son Michael.

COURSES

  • Cell Biology (will be comibined with Molecular Biology starting Fall of 2013)
  • Fundamentals of Plant Biochemistry/Pathology
  • Bio-separations: Principles and Practices (With Dr. Michael A. Savka)

CONTACT INFORMATION

André O. Hudson, Ph.D.
Assistant Professor
Thomas H. Gosnell School of Life Sciences
Rochester Institute of Technology
85 Lomb Memorial Drive
Rochester, NY 14623
Phone: 585-475-4259
Fax:585-475-5766
aohsbi@rit.edu

CURRENT RESEARCH IN THE HUDSON LAB

1. Amino Acid Metbolism

My laboratory is primarily interested in amino acid metabolism. More specifically, we are interested in the aminotransferases class of enzyme. Aminotranferases or transaminases (EC 2.6.1.x) are ubiquitous enzymes that are involved in amino acid biosynthesis, vitamin metabolism, carbon and nitrogen assimilation, secondary metabolism etc. They catalyze reversible reactions by transferring an amine group from a donor to an acceptor. The amino donor is usually an amino acid and the amino acceptor is usually a 2-oxo-acid. In the model organism Arabidopsis thaliana, there are 44 annotated aminotransferases many of which are uncharacterized. Using biochemical and bio-informatical approaches, my lab is interested in elucidating the function of the remaining aminotransferase enzymes that are deemed putative from organisms such as; plants, bacteria and algae.

2. Structural analysis of enzymes involved in amino acid metabolism
(with Dr. Renwick C.J. Dobson-University of Canterbury)

Some of the enzymes involved in the metabolism of amino acids are putative or validated antibiotic targets based on the fact these amino acids are essential for the growth and development of animals particularly humans. The Hudson lab is currently collaborating with the lab of Dr. Renwick Dobson from the University of Canterbury to elucidate the 3-dimensional structure of enzymes involved in amino acid metabolism.

3. Bacterial Endophytes
(with Dr. Michael A. Savka-Rochester Institute of Technology)

A collaborative project with Dr. Michael Savka (GSOLS) to assess the role(s) of endophytic bacteria from plants such as sugarcane and grapes is under way. Recently, the genomes of three bacterial endophytes were sequenced and annotated by our groups with collaborator Dr. Han Ming Gan. One of the goals of the project is to elucidate the symbiotic relationship betweeen the plant and the bacterium in question.

Students in my laboratory will be exposed to a variety of techniques from many disciplines including; biochemistry, molecular biology, enzymology, microbiology, plant biology/pathology, evolutionary biology, structural biology among others. Email aohsbi@rit.edu to inquire about research opportunities.

Acknowledgements

I would like to thank the National Science Foundation (NSF), The RIT College of Science (COS), The Thomas H. Gosnell School of Life Sciences (GSOLS), The RIT Office of the Vice President for Research (OVPR) and Sweetwater Energy (Rochester NY) for financial support. I would also like to thank all the wonderful collaborators and undergraduate students throughout the years.


The relative map positions of aminotransferase and aminotransferase-like genes disrtibuted on the 5 chromosomes of Arabidopsis thaliana


The dimeric structure of diaminopimelate aminotransferase
from the alga C. reinhardtii solved by the Hudson and Dobson groups.