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Agrobacterium tumefaciens and A. rhizogenes use different proteins to transport bacterial DNA into the plant cell nucleus.

Ream W - Microb Biotechnol (2009)

Bottom Line: Unlike VirE2, GALLS-FL contains ATP-binding and helicase motifs similar to those in TraA, a strand transferase involved in conjugation.GALLS-FL accumulates inside the nucleus where its predicted ATP-dependent strand transferase may pull T-strands into the nucleus.These different mechanisms for nuclear import of T-strands may affect the efficiency and quality of transgenic events in plant biotechnology applications.

View Article: PubMed Central - PubMed

Affiliation: Department of Microbiology, Oregon State University, Corvallis, OR 97331, USA. reamw@orst.edu

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Mentions: Full‐length GALLS (GALLS‐FL) (Hodges et al., 2006) and VirE2 (Vergunst et al., 2000; 2003; Simone et al., 2001) contain C‐terminal signals for translocation into plant cells mediated by the VirB/D4 type IV secretion system (Fig. 1). VirE2 contains two NLSs (Citovsky et al., 1992; Zupan et al., 1996), whereas GALLS‐FL contains a single bipartite NLS (Fig. 1) (Hodges et al., 2004), which is important for its ability to substitute for VirE2 (Hodges et al., 2006). This indicates that GALLS‐FL performs a critical function inside the nucleus or at the nuclear membrane, as does VirE2.


Agrobacterium tumefaciens and A. rhizogenes use different proteins to transport bacterial DNA into the plant cell nucleus.

Ream W - Microb Biotechnol (2009)

© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815903&req=5

Mentions: Full‐length GALLS (GALLS‐FL) (Hodges et al., 2006) and VirE2 (Vergunst et al., 2000; 2003; Simone et al., 2001) contain C‐terminal signals for translocation into plant cells mediated by the VirB/D4 type IV secretion system (Fig. 1). VirE2 contains two NLSs (Citovsky et al., 1992; Zupan et al., 1996), whereas GALLS‐FL contains a single bipartite NLS (Fig. 1) (Hodges et al., 2004), which is important for its ability to substitute for VirE2 (Hodges et al., 2006). This indicates that GALLS‐FL performs a critical function inside the nucleus or at the nuclear membrane, as does VirE2.

Bottom Line: Unlike VirE2, GALLS-FL contains ATP-binding and helicase motifs similar to those in TraA, a strand transferase involved in conjugation.GALLS-FL accumulates inside the nucleus where its predicted ATP-dependent strand transferase may pull T-strands into the nucleus.These different mechanisms for nuclear import of T-strands may affect the efficiency and quality of transgenic events in plant biotechnology applications.

View Article: PubMed Central - PubMed

Affiliation: Department of Microbiology, Oregon State University, Corvallis, OR 97331, USA. reamw@orst.edu

Show MeSH