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. 2010 Mar 26;192(11):2830–2838. doi: 10.1128/JB.01331-09

FIG. 2.

FIG. 2.

A VirB3-VirB4 fusion protein is functional in DNA transfer to plants. (A) Complementation of Agrobacterium A348ΔB3 (ΔB3) and A348ΔB4 (ΔB4) was monitored by tumor formation assays. Plasmid pB34 (pAD1888) expresses a virB3-virB4 fusion, and plasmid pB3B4 (pAD1887) expresses wild-type virB3 and virB4. Both plasmids express virB1 and virB2 as well. (B) Expression of VirB3-VirB4 fusion and other VirB proteins was monitored by Western blot assays. Proteins were separated by electrophoresis in SDS-10% PA gels (VirB4 and VirB3-VirB4 fusion) or SDS-12.5% PA-Tricine gels (VirB3 and VirB10). Arrowheads identify the VirB3-VirB4 fusion bands (lanes 5 and 8) and the weak VirB3 bands in two of the A348ΔB4 derivatives (lanes 6 and 8). Note that no VirB3-specific band is detectable for A348ΔB3/pB34, which expresses the VirB3-VirB4 fusion protein (lane 5). A protein migrating slightly slower than VirB3 cross-reacted nonspecifically with the anti-VirB3 antibodies. VirB3 expression was high in wild-type A348 and in bacteria expressing virB3 from a plasmid (lanes 2, 4, and 7). The lower bands in both the VirB3 and VirB10 blots are degradation products. Lane C, induced A348ΔB.