Abstract
ABSTRACTAgrobacterium tumefaciens has the ability to transform a wide range of eukaryotes by transferring single-stranded (ss) DNA (T-DNA) into the host cells. During the process, the bacterium also delivers abundant amount of ssDNA binding protein VirE2 into the host cytoplasm, where multiple VirE2 molecules bind and coat the T-DNA and thus generate large-sized nucleoprotein complex. VirE2 trafficking should be representative of T-DNA movement. Recently, we demonstrated that plant actomyosin motility system facilitated the trafficking of Agrobacterium-delivered VirE2 inside host cytoplasm. We showed that actomyosin-driven VirE2 moved towards the nucleus along the endoplasmic reticulum (ER). Here we hypothesize that the presence of VirE2 on the cytoplasmic side of the ER may provide VirE2 with convenient access to the opening of nuclear pore complexes (NPCs). We propose models to explain how VirE2 is trafficked in the context of actin, myosin and ER.
Highlights
Agrobacterium tumefaciens has the ability to transform a wide range of eukaryotes by transferring single-stranded DNA (T-DNA) into the host cells
We demonstrated that VirE2 is trafficked inside plant cytoplasm via a myosin XI-K-powered endoplasmic reticulum (ER)/actin network.[10]
The GFP1–10 fragment localized inside the ER lumen did not complement the bacterium-delivered VirE2-GFP11, suggesting that the VirE2 is on the cytosolic side of the ER
Summary
Agrobacterium tumefaciens has the ability to transform a wide range of eukaryotes by transferring single-stranded (ss) DNA (T-DNA) into the host cells. KEYWORDS VirE2; protein trafficking; myosin; endoplasmic reticulum; actin filaments VirD2-T-DNA complex is delivered together with other virulence proteins into host cells.[5] Inside plant cells, the VirD2-bound T-DNA is coated by ssDNA
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