It is customary in these introductions to speak of the work
of the award recipient and I shall attend to that shortly. But first I
want to speak of Paul’s personal history and his character because
that profoundly colors the kind of work he does, the kind of teacher he
strives to be and the high level of insight and breadth he brings to
his work. In all of this, he is truly a “Marathon Man.”
Paul was born in Palmyra, New York, and demonstrated an early interest
in science. For example, after attending a summer science program at
Bar Harbor, he brought some mice home (rules were simpler then) to
continue studies in his garage on folate and teratology. He ultimately
graduated from Colgate University, magna cum laude with
honors in Chemistry and Phi Beta Kappa. After a year of graduate
school, the lust for travel and teaching expressed itself and he left
for East Africa in the AID program (Agency for International
Development), a precursor to the Peace Corps. There, he obtained
certification as a teacher and taught chemistry, physics and math at
the Friend’s School in Kenya. After two years, he toured the Middle
East and Europe and then returned to resume graduate work in
biochemistry, joining Dr. Finn Wold’s laboratory, at Illinois. There,
he met his lovely and talented wife Doris, and they moved to
Minneapolis as the lab moved to the University of Minnesota. During
this time, he became an accomplished protein chemist. He was able to
utilize these skills to great advantage in his Postdoctoral Position
with Dr. William J. Dreyer at Caltech where I had also began my career
in Vision Research the year before. With a laboratory focus on
photoreceptor membranes, Paul took over the study of rhodopsin’s amino
acid sequence.
Now a bit about his character. He goes the distance - he finishes the
race. I do not use the title Marathon Man only as a metaphor. He has
run 38 marathons, his last just before this meeting in London. He’s
run the Boston Marathon three times and has a personal goal of
completing a marathon in every state (he’s currently completed 28 with
22 to go). He’s been a nurturing father and husband. Paul and Doris’
daughter, Elizabeth, now 28, completed her graduate work at UT Austin
and now has joined Sen. Daschle’s office staff in Washington, D. C. Their son, David, is currently a college student performing in the
family tradition with excellent studies. When Doris turned 40, she
decided to resume her education. She attended Law School in Gainesville
and Paul kicked her out of the house to go to the library while he did
the shopping, cooking and much of the parenting. She now has a
successful practice in family law there.
Paul speaks quietly, and moves carefully. There is little of the
showman in his personality. But if you listen, you hear a marathon man
at work. No stone is left unturned. The scientific papers are never
published hurriedly. They are always complete, correct, and make a huge
impact in our field. He is generous and comprehensive in his
acknowledgment of the work of others. He has an extraordinary record of
accomplishment as an educator of teachers and scientists.
In his research, Paul, Dr. S-L Fong and his close and long-time
colleague, Dr. J. Hugh McDowell, worked together in the earliest years,
first at Southern Illinois University Medical School in Carbondale, and
then at the University of Florida at Gainesville. Throughout the
1970’s and early 80’s, their effort was to comprehensively isolate,
sequence and order all the peptides of rhodopsin into the form we all
understand today. To those of you who were not yet born in 1970,
perhaps I should remind you of how formidable a task this was then. We
didn’t have molecular biology, no cDNA’s, blots or mass
spectrometers. The amino acid analyzers were sensitive only to the
millimolar range. Automated sequencers worked well on abundant
water-soluble peptides, but the purification of water-insoluble
peptides, of which there are many in rhodopsin, was an enormous
problem. Many of his papers on the way to completing rhodopsin’s
sequence shared their discoveries about how to manage these peptides
arising from the intractable intramembranous domains of rhodopsin. With
time though, as the structure of rhodopsin became clear, the field
became more rational. Now studies could be explicitly designed to
determine which domains became phosphorylated by rhodopsin kinase and
which loops bound transducin. His wanderlust, never leaving him,
brought him to Poland where he met and entranced Kris Palczewski and
Gryzyna Adamus. He brought them to his lab for a most successful
postdoctoral experience and launched them on their own distinguished
careers. Making monoclonal antibodies to map the surfaces of rhodopsin
and its modifications by phosphorylation, they also launched the
analysis of rhodopsin’s partners, rhodopsin kinase, transducin,
arrestin and protein phosphatase 2A, thereby helping in the
international effort to clarify both signal amplification and dark
adaptation of rhodopsin.
Suddenly, in the late 80’s with the arrival of molecular biological
techniques, work on rhodopsin greatly expanded. Numerous membrane
proteins interacting with trimeric G-proteins were isolated and found
to be structurally related to rhodopsin. The decades of work on
rhodopsin’s primary structure and the details of the visual cycle
became the model for the action of the adrenergic receptors, and then
dopamine, cannabinoid, substance P, and literally hundreds of other
receptors, even the mating type receptors of chlamydomonas. It became
obvious that rhodopsin belonged to a huge and ancient family adapted
freely by evolution to conduct the business of sensing the physical and
chemical environment and transducing the information usefully to the
cell and the organism. Paul’s group conducted comparative studies of
sequences of widely divergent rhodopsins, including Florida alligators
and ants! He, of course, went out on the hunt. You can well imagine the
satisfaction that swept over his friends when the discovery that
rhodopsin mutations initiate autosomal dominant retinitis pigmentosa
was announced at ARVO in 1989 by Drs. Ted Dryja and Eliot Berson and
their colleagues. Paul’s model was up on the screen and the P23H
mutation was identified. Now over 70 different mutations and
polymorphisms have been identified in human rhodopsin and the
clinical-molecular correlation is still a lively subject for clinicians
and scientists. So his work was brought to the ophthalmology clinic.
In addition to all this outstanding laboratory effort, Paul has
served the vision community as a Biochemistry Section chairman of ARVO,
a member and Chair of the VisA2 Visual Disorders Study Section and as
an organizer of FASEB conferences and numerous international symposia.
He has edited several volumes of papers on vision. A loyal faculty
member, he has not shirked academic responsibility, taking his turn
chairing his department at SIU, serving on search committees and
Directing the Core Facility for Vision Research at Gainesville. His
loyalty and accomplishments have not gone unnoticed. He came to
Gainesville as a Jules and Doris Stein Research to Prevent Blindness
Professor and in 1990 was named the Francis N. Bullard Professor and
Eminent Scholar of Ophthalmology and Biochemistry. They also conferred
numerous awards for his achievements in research, the latest, the
University of Florida Superior Accomplishment Award this year. He has
been continuously supported by NIH awards since first establishing his
independent laboratory at SIU.
Now, Paul is back in airplanes and pounding the roads again–for both
personal and scientific reasons. He’s off to Cambridge, England to
work with the Shertler group to determine the three-dimensional shape
of rhodopsin. Like all fine marathon runners, steep slopes are seen
simply as nature’s way to test you and determine what sort of finisher
you really are. Luckily for us, Paul has more races to run. We can look
confidently forward to him arriving at the scientific finish line, on
time, looking ahead with anticipation to the next race.