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Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):10108-13. Epub 2003 Aug 4.

The VirD2 pilot protein of Agrobacterium-transferred DNA interacts with the TATA box-binding protein and a nuclear protein kinase in plants.

Author information

1
Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, D-50829 Cologne (Köln), Germany.

Abstract

The bacterial virulence protein VirD2 plays an important role in nuclear import and chromosomal integration of Agrobacterium-transferred DNA in fungal, plant, animal, and human cells. Here we show that in nuclei of alfalfa cells, VirD2 interacts with and is phosphorylated by CAK2Ms, a conserved plant ortholog of cyclin-dependent kinase-activating kinases. CAK2Ms binds to and phosphorylates the C-terminal regulatory domain of RNA polymerase II largest subunit, which can recruit the TATA box-binding protein. VirD2 is found in tight association with the TATA box-binding protein in vivo. These results indicate that recognition of VirD2 is mediated by widely conserved nuclear factors in eukaryotes.

PMID:
12900506
PMCID:
PMC187781
DOI:
10.1073/pnas.1733208100
[Indexed for MEDLINE]
Free PMC Article

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