I was born in the island of Jamaica and grew up in the town of Savanna-La-Mar in the parish of Westmoreland (see map below). I came to the United States at the age of 14 and completed High School at Salesian High in New Rochelle, NY. I received 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 aimed at identifying pathogenic
bacteria from fresh farm produce. I completed my Ph.D. in the department of Plant Biology and Pathology in 2006 under the direction of Dr. Thomas Leustek at Rutgers University. I joined the faculty in the School of Life Sciences in the Fall of 2008 following a post-doctoral fellowship at Rutgers. I am a member of Alpha Phi Alpha Fraternity, Inc. (Gamma Chapter-VUU Spring 1998). I love music (authentic reggae-Bob Marley, Peter Tosh, Burning Spear etc.), reading (autobiographies), chess and sports (football-Bills), (soccer-Brazil), (baseball-Yankees), (basketball-Knicks).
I reside in Hilton, New York with my wife Candice and my son Michael (7).
- Cellular and Molecular Biology-Fall 2014-15
- Fundamentals of Plant Biochemistry/Pathology Fall 2014-15
- Bio-separations: Principles and Practices (with Dr. Michael Savka) Spring 2014-2015
- Molecular Ecology (with Dr. Sandi Connelly)TBA
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- Institute Calendar
André O. Hudson, Ph.D.
Thomas H. Gosnell School of Life Sciences
Rochester Institute of Technology
85 Lomb Memorial Drive
Rochester, NY 14623
Office: Gosnell Hall (Bldg 08) Room A358
Lab: Gosnell Hall (Bldg 08) Room A355
CURRENT RESEARCH IN THE HUDSON LAB
Amino Acid Metabolism
My laboratory is primarily interested in amino acid metabolism. More specifically, we are interested in the aminotransferase class of enzyme. Aminotransferases 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 amino 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.
Various organisms used in the Hudson lab
The relative map positions of aminotransferase and aminotransferase-like genes distributed on the 5 chromosomes of Arabidopsis thaliana
Transamination interconverts pairs of amino acids and keto acids. During transamination, the amino group of an amino acid is transferred to a keto acid, this produces a new keto acid while from the original keto acid, a new amino acid is formed. The enzyme employs a ping-pong (double displacement)(see cartoon above) mechanism facilitated by the co-factor pyridoxal phosphate (PLP) which is bound to a conserved lysine residue in the active site of the enzyme.
Structural analyses 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 bacterial growth and the anabolic pathways are absent in 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.
The dimeric structure of diaminopimelate aminotransferase
from the alga C. reinhardtii
solved by the Hudson and Dobson groups.
Homology model of V. spinosum
Homolgy model of meso-diaminopimelate ligase (MurEVs).(a) The homology model of MurEVs highlighting domains A (grey), B (violet) and C (pink). (b) Shows the structure model of MurEVs bound to UDP-MurNAc-tripeptide (UMT) product (yellow). (c) Active site residue hypothesized to bind to UMT product is shown in red. The structure has been rotated 90 degrees on the right panel for the better viewing of the binding pocket. (d) Cross eye stereo view showing the interaction between amino acid residues of the binding site and UMT product.
Indentifcation of Bacterial Endophytes/Epiphytes
(Dr. Michael A. Savka-Rochester Institute of Technology)
(Dr. Larry Smart-Cornell University)
A collaborative project with Dr. Michael Savka (GSOLS) to identify and assess the role(s) of endophytic and epiphytic bacteria from plants such as sugarcane and grape is under way.
We recently forged a collabortion with Dr. Larry Smart from Cornell University Department of Horiticulture to identify endophytes from willow.
Isolation and identification of bacterial endophytes from sugarcane using 16S V3 rDNA analysis
Recently, the genomes of 19 plant associated bacteria fromw sugarcane, yam and willow were sequenced and annotated in collaboration with Dr. Han Ming Gan (Monash University, Malaysia).
I am always interested in having enthusiastic and passionate students in my laboratory if there are openings. 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 me at firstname.lastname@example.org
to inquire about research opportunities.
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.