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THE PLANT CELL, Vol 6, Issue 3 405-416, Copyright © 1994 by American Society of Plant Biologists
Geminivirus Replication Origins Have a Modular Organization
EPB. Fontes, H. J. Gladfelter, R. L. Schaffer, ITD. Petty and L. Hanley-Bowdoin
Department of Biochemistry, P.O. Box 7622, North Carolina State University, Raleigh, North Carolina 27695-7622
Tomato golden mosaic virus (TGMV) and bean golden mosaic virus (BGMV) are
closely related geminiviruses with bipartite genomes. The A and B DNA
components of each virus have cis-acting sequences necessary for
replication, and their A components encode trans-acting factors required
for this process. We showed that virus-specific interactions between the
cis- and trans-acting functions are required for TGMV and BGMV replication
in tobacco protoplasts. We also demonstrated that, similar to the essential
TGMV AL1 replication protein, BGMV AL1 binds specifically to its origin in
vitro and that neither TGMV nor BGMV AL1 proteins bind to the heterologous
origin. The in vitro AL1 binding specificities of the B components were
exchanged by site-directed mutagenesis, but the resulting mutants were not
replicated by either A component. These results showed that the
high-affinity AL1 binding site is necessary but not sufficient for
virus-specific origin activity in vivo. Geminivirus genomes also contain a
stem-loop sequence that is required for origin function. A BGMV B mutant
with the TGMV stem-loop sequence was replicated by BGMV A, indicating that
BGMV AL1 does not discriminate between the two sequences. A BGMV B double
mutant, with the TGMV AL1 binding site and stem-loop sequences, was not
replicated by either A component, indicating that an additional element in
the TGMV origin is required for productive interaction with TGMV AL1. These
results suggested that geminivirus replication origins are composed of at
least three functional modules: (1) a putative stem-loop structure that is
required for replication but does not contribute to virus-specific
recognition of the origin, (2) a specific high-affinity binding site for
the AL1 protein, and (3) at least one additional element that contributes
to specific origin recognition by viral trans-acting factors.
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