| Literature DB >> 19513263 |
Benoît Lacroix1, Vitaly Citovsky.
Abstract
Agrobacterium genetically transforms its hosts by transferring a segment of DNA (T-DNA) into the host cell and integrating it into the host genome. Integration requires a close interaction between T-DNA, which is packaged into a nucleoprotein complex (T-complex) by bacterial virulence (Vir) proteins, and the host chromatin. This interaction is facilitated by the host protein VIP 1, which binds both to the major protein component of the T-complex, VirE2, and to the core histones. Recently, VIP1 has been demonstrated to mediate the interaction between plant nucleosomes and VirE2-DNA complexes (i.e., synthetic T-complex-like structures) in vitro. Here, we discuss major implications of these observations-such as the possible role of core histone modifications, proteasomal uncoating of the T-complex mediated by the bacterial F-box protein VirF, and the need for changes in chromatin structure to render it accessible to the T-DNA integration-for the process of chromatin targeting of foreign DNA and its integration into the eukaryotic genome.Entities:
Keywords: T-complex; VirE2; VirE2-interacting protein 1 (VIP1); chromatin targeting; histones; nucleosomes
Year: 2009 PMID: 19513263 PMCID: PMC2649301 DOI: 10.4161/cib.2.1.7468
Source DB: PubMed Journal: Commun Integr Biol ISSN: 1942-0889