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RESEARCH SUMMARY
The research program of
the lab involves understanding the fundamental
structure ® function relationships of RNases
H with the long term goals of a) unmasking
novel nucleic acid metabolic functions associated
with the enzymes and b) understanding their
placement in the replicative life cycle
of the pathogenic protozoan Trypanosoma
brucei. Trypanosomes are amongst the
earliest branching eukaryotes and are the
models in which RNA editing and trans-splicing
were initially discovered. Accordingly,
they are well suited for our studies.
Viral RNases H are also being evaluated
as potential therapeutic targets and our
studies emphasize identifying RNase H mutations
which may account for drug resistance during
the course of drug treatment. RNases H are
widely distributed nucleic acid metabolic
enzymes which degrade the RNA strand of
RNA:DNA heteroduplexes. They are also utilized
by all biological systems. Our current models
are excellent platforms from which to move
and study these enzymes in related systems.
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PUBLICATIONS
Campbell, AG (2001).
Expression of Moloney Murine Leukemia Virus
RNase H Rescue the Growth defect of an Escherichia
coli Mutant. J. Virology 75:13 6212-6217.
Kobil, J. H and A. G. Campbell. (2000)
Functional Analysis of the Domain Organization
of Trypanosoma brucei RNase HI. Biochem.
Biophys. Res. Commun., 270:336-342.
Kobil, J. H and A. G. Campbell.
(2000) Trypanosoma brucei RNase HI
Requires its Divergent Spacer Subdomain
for Enzymatic Function and its RNA Binding
Motif for Nuclear Localization. Molec.
Biochem. Parasitol., 107:135-142.
Hesslein, D.G.T. and A. G. Campbell.
(1997) Molecular Cloning and Expression
of a Ribonuclease H from the Kinetoplastid,
Trypanosoma brucei., Molec.
Biochem. Parasitol., 86:121-126.
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