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J Biol Chem, Vol. 275, Issue 9, 6114-6122, March 3, 2000
From the Department of Biochemistry, North Carolina State
University, Raleigh, North Carolina 27695-7622
Tomato golden mosaic virus (TGMV), a member of
the geminivirus family, encodes one essential replication protein, AL1,
and recruits the rest of the DNA replication apparatus from its plant host. TGMV AL1 is an oligomeric protein that binds double-stranded DNA
and catalyzes cleavage and ligation of single-stranded DNA. The
oligomerization domain, which is required for DNA binding, maps to a
region that displays strong sequence and structural homology to other
geminivirus Rep proteins. To assess the importance of conserved
residues, we generated a series of site-directed mutations and analyzed
their impact on AL1 function in vitro and in
vivo. Two-hybrid experiments revealed that mutation of amino acids 157-159 inhibited AL1-AL1 interactions, whereas mutations at
nearby residues reduced complex stability. Changes at positions 157-159 also disrupted interaction between the full-length mutant protein and a glutathione S-transferase-AL1 oligomerization
domain fusion in insect cells. The mutations had no detectable effect on oligomerization when both proteins contained full-length AL1 sequences, indicating that AL1 complexes can be stabilized by amino
acids outside of the oligomerization domain. Nearly all of the
oligomerization domain mutants were inhibited or severely attenuated in
their ability to support AL1-directed viral DNA replication. In
contrast, the same mutants were enhanced for AL1-mediated transcriptional repression. The replication-defective AL1 mutants also
interfered with replication of a TGMV A DNA encoding wild type AL1.
Full-length mutant AL1 was more effective in the interference assays
than truncated proteins containing the oligomerization domain.
Together, these results suggested that different AL1 complexes mediate
viral replication and transcriptional regulation and that replication
interference involves multiple domains of the AL1 protein.
The Multifunctional Character of a Geminivirus Replication
Protein Is Reflected by Its Complex Oligomerization Properties*
,
*
This work was supported by Grant MCB-9809953 (to L. H.-B.) from the National Science Foundation and the DuPont Company
(Educational Aid Grant program).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 919-515-5736;
Fax: 919-515-2047.
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