2004
DOI: 10.1111/j.1365-313x.2004.02041.x
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Nuclear localization and interaction of RolB with plant 14‐3‐3 proteins correlates with induction of adventitious roots by the oncogene rolB

Abstract: SummaryThe rooting-locus gene B (rolB) on the T-DNA of the root-inducing (Ri) plasmid in Agrobacterium rhizogenes is responsible for the induction of transformed adventitious roots, although the root induction mechanism is unknown. We report here that the RolB protein of pRi1724 (1724RolB) is associated with Nicotiana tabacum 14-3-3-like protein vII (Nt14-3-3 vII) in tobacco bright yellow (BY)-2 cells. Nt14-3-3 vII directly interacts with 1724RolB protein. Green¯uorescent protein (GFP)-fused 1724RolB is locali… Show more

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Cited by 74 publications
(47 citation statements)
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References 76 publications
(116 reference statements)
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“…Exoenzyme S, an ADP-ribosyl-transferase toxin secreted by the TTSS of Pseudomonas aeruginosa, becomes active upon interaction with host 14-3-3 proteins (Ottmann et al, 2007). The nuclear accumulation of RolB, a bacterial oncoprotein involved in the pathogenesis of Agrobacterium rhizogenes, depends upon binding to a specific isoform of 14-3-3 (Moriuchi et al, 2004). Based on in silico predictions, HopQ1 is classified as a nucleoside hydrolase; however, this activity could not be detected in the recombinant protein produced in E. coli.…”
Section: Discussionmentioning
confidence: 99%
“…Exoenzyme S, an ADP-ribosyl-transferase toxin secreted by the TTSS of Pseudomonas aeruginosa, becomes active upon interaction with host 14-3-3 proteins (Ottmann et al, 2007). The nuclear accumulation of RolB, a bacterial oncoprotein involved in the pathogenesis of Agrobacterium rhizogenes, depends upon binding to a specific isoform of 14-3-3 (Moriuchi et al, 2004). Based on in silico predictions, HopQ1 is classified as a nucleoside hydrolase; however, this activity could not be detected in the recombinant protein produced in E. coli.…”
Section: Discussionmentioning
confidence: 99%
“…The localization of these proteins in plant cells is also different. HopAO1 is localized to the soluble fraction of protein extracts (Underwood et al, 2007), whereas RolB is localized in the plasma membrane (Filippini et al, 1996) or in the nucleus (Moriuchi et al, 2004). Therefore, these proteins have probably evolved independently.…”
Section: Similarity and Dissimilarity Between Rolb-and Pseudomonas Symentioning
confidence: 99%
“…The mechanism by which the RolB oncoprotein exerts such different morphological alterations remains unknown. RolB was shown to exhibit Tyr phosphatase activity (Filippini et al, 1996) and interact with 14-3-3 proteins (Moriuchi et al, 2004). RolB has no homology to any prokaryotic or eukaryotic proteins except the RolB (PLAST) family of oncoproteins in Agrobacterium species (Levesque et al, 1988;Otten and Schmidt, 1998).…”
mentioning
confidence: 99%
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“…A survey involving 10 14-3-3 genes from tomato showed that three were induced by the Cf9-mediated hypersensitive defense response (Roberts and Bowles, 1999). A final example is that of 14-3-3 proteins suggested in Agrobacterium rhizogenes to bind RolB and direct it to the nucleus (Moriuchi et al, 2004).…”
mentioning
confidence: 99%