@article{arguello-astorga_lopez-ochoa_kong_orozco_settlage_hanley-bowdoin_2004, title={A novel motif in geminivirus replication proteins interacts with the plant retinoblastoma-related protein}, volume={78}, ISSN={["1098-5514"]}, DOI={10.1128/JVI.78.9.4817-4826.2004}, abstractNote={ABSTRACT}, number={9}, journal={JOURNAL OF VIROLOGY}, author={Arguello-Astorga, G and Lopez-Ochoa, L and Kong, LJ and Orozco, BM and Settlage, SB and Hanley-Bowdoin, L}, year={2004}, month={May}, pages={4817–4826} }
 @misc{hanley-bowdoin_orozco_kong_gruissem_2004, title={Geminivirus resistant transgenic plants}, volume={6,800,793}, number={2004 Oct. 5}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Hanley-Bowdoin, L. and Orozco, B. M. and Kong, L. J. and Gruissem, W.}, year={2004} }
 @article{castillo_kong_hanley-bowdoin_bejarano_2004, title={Interaction between a geminivirus replication protein and the plant sumoylation system}, volume={78}, ISSN={["1098-5514"]}, DOI={10.1128/JVI.78.6.2758-2769.2004}, abstractNote={ABSTRACT}, number={6}, journal={JOURNAL OF VIROLOGY}, author={Castillo, AG and Kong, LJ and Hanley-Bowdoin, L and Bejarano, ER}, year={2004}, month={Mar}, pages={2758–2769} }
 @article{kong_hanley-bowdoin_2002, title={A geminivirus replication protein interacts with a protein kinase and a motor protein that display different expression patterns during plant development and infection}, volume={14}, ISSN={["1532-298X"]}, DOI={10.1105/tpc.003681}, abstractNote={The geminivirus protein AL1 initiates viral DNA replication, regulates its own expression, and induces plant gene transcription. To better understand how AL1 interacts with host proteins during these processes, we used yeast two-hybrid library screening and a baculovirus protein interaction system to identify plant proteins that interact with AL1. These studies identified a Ser/Thr kinase, a kinesin, and histone H3 as AL1 partners. The kinase is autophosphorylated and can phosphorylate common kinase substrates in vitro. The kinesin is phosphorylated in insect cells by a cyclin-dependent kinase. Immunostaining of Nicotiana benthamiana and Arabidopsis showed that kinase protein levels and subcellular location are regulated during plant development and geminivirus infection. By contrast, the kinesin is ubiquitous even though it is associated with the spindle apparatus in mitotic cells. Together, our results establish that AL1 interacts with host proteins involved in plant cell division and development. Possible functions of these host factors in healthy and geminivirus-infected plants are discussed.}, number={8}, journal={PLANT CELL}, author={Kong, LJ and Hanley-Bowdoin, L}, year={2002}, month={Aug}, pages={1817–1832} }
 @article{kong_orozco_roe_nagar_ou_feiler_durfee_miller_gruissem_robertson_et al._2000, title={A geminivirus replication protein interacts with the retinoblastoma protein through a novel domain to determine symptoms and tissue specificity of infection in plants}, volume={19}, ISSN={["0261-4189"]}, DOI={10.1093/emboj/19.13.3485}, abstractNote={Geminiviruses replicate in nuclei of mature plant cells after inducing the accumulation of host DNA replication machinery. Earlier studies showed that the viral replication factor, AL1, is sufficient for host induction and interacts with the cell cycle regulator, retinoblastoma (pRb). Unlike other DNA virus proteins, AL1 does not contain the pRb binding consensus, LXCXE, and interacts with plant pRb homo logues (pRBR) through a novel amino acid sequence. We mapped the pRBR binding domain of AL1 between amino acids 101 and 180 and identified two mutants that are differentially impacted for AL1–pRBR interactions. Plants infected with the E‐N140 mutant, which is wild‐type for pRBR binding, developed wild‐type symptoms and accumulated viral DNA and AL1 protein in epidermal, mesophyll and vascular cells of mature leaves. Plants inoculated with the KEE146 mutant, which retains 16% pRBR binding activity, only developed chlorosis along the veins, and viral DNA, AL1 protein and the host DNA synthesis factor, proliferating cell nuclear antigen, were localized to vascular tissue. These results established the importance of AL1–pRBR interactions during geminivirus infection of plants.}, number={13}, journal={EMBO JOURNAL}, author={Kong, LJ and Orozco, BM and Roe, JL and Nagar, S and Ou, S and Feiler, HS and Durfee, T and Miller, AB and Gruissem, W and Robertson, D and et al.}, year={2000}, month={Jul}, pages={3485–3495} }
 @article{orozco_kong_batts_elledge_hanley-bowdoin_2000, title={The multifunctional character of a geminivirus replication protein is reflected by its complex oligomerization properties}, volume={275}, ISSN={["0021-9258"]}, DOI={10.1074/jbc.275.9.6114}, abstractNote={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.}, number={9}, journal={JOURNAL OF BIOLOGICAL CHEMISTRY}, author={Orozco, BM and Kong, LJ and Batts, LA and Elledge, S and Hanley-Bowdoin, L}, year={2000}, month={Mar}, pages={6114–6122} }