@article{pedersen_hanley-bowdoin_1994, title={Molecular Characterization of the AL3 Protein Encoded by a Bipartite Geminivirus}, volume={202}, ISSN={0042-6822}, url={http://dx.doi.org/10.1006/viro.1994.1442}, DOI={10.1006/viro.1994.1442}, abstractNote={The genome of tomato golden mosaic virus (TGMV) is composed of two circular, single-stranded DNA molecules that together contain 6 open reading frames (ORFs). Three of these ORFs (designated AL1, AL2, and AL3) overlap and are specified by multiple polycistronic mRNAs. No RNA specifying the AL3 ORF alone has been detected, suggesting that the AL3 gene product is translated from an internal ORF. A recombinant histidine-tagged-AL3 fusion protein was purified from Escherichia coli and used to raise a polyclonal antiserum. Analysis of protein extracts from healthy plants and plants infected with TGMV by SDS-PAGE and immunoblotting showed that a protein corresponding to the predicted AL3 gene product is produced only in infected plants. This protein comprises approximately 0.05% of the cellular proteins and is present in the soluble and organelle fractions. These results are discussed with respect to the expression and role of the AL3 protein in the viral life cycle.}, number={2}, journal={Virology}, publisher={Elsevier BV}, author={Pedersen, Thomas J. and Hanley-Bowdoin, Linda}, year={1994}, month={Aug}, pages={1070–1075} }
 @article{pedersen_arwood_spiker_guiltinan_thompson_1991, title={High mobility group chromosomal proteins bind to AT-rich tracts flanking plant genes}, volume={16}, ISSN={0167-4412 1573-5028}, url={http://dx.doi.org/10.1007/bf00017920}, DOI={10.1007/BF00017920}, abstractNote={AT-rich sequences in the 5' flanking regions of several plant genes have been shown to bind nuclear proteins, but the nature of these proteins has remained largely unknown. We report here that certain plant high mobility group (HMG) chromosomal proteins can interact specifically (in the presence of excess non-specific competitor) with AT-rich sequences located upstream of the pea ferredoxin 1 gene (Fed-1) and a member of the wheat Em gene family. Binding was observed with highly purified preparations of HMGa or HMGb, but not with HMGc or HMGd. HMG-DNA complexes were similar to one of the two types of Fed-1 complexes we observed previously using pea nuclear extracts [7]. HMG binding to the Fed-1 DNA was localized to a region containing AT-rich sequences; very similar sequences are present 5' to Em and several other plants genes. Such sequences have been shown to bind unidentified nuclear proteins in a number of these systems. Binding experiments with a synthetic oligo (dA).oligo (dT) probe and competition experiments with synthetic DNA polymers suggest that HMG binding may depend upon structural features of AT-rich DNA rather than being sequence-specific. We discuss the implications of these findings and suggest a role for HMG binding which is consistent with previous evidence linking HMGs with transcriptionally competent chromatin.}, number={1}, journal={Plant Molecular Biology}, publisher={Springer Nature America, Inc}, author={Pedersen, Thomas J. and Arwood, Laura J. and Spiker, Steven and Guiltinan, Mark J. and Thompson, William F.}, year={1991}, month={Jan}, pages={95–104} }