scholarly journals Characterization of a putative periplasmic transport system for octopine accumulation encoded by Agrobacterium tumefaciens Ti plasmid pTiA6.

1991 ◽  
Vol 173 (20) ◽  
pp. 6398-6405 ◽  
Author(s):  
R H Valdivia ◽  
L Wang ◽  
S C Winans
1990 ◽  
Vol 265 (8) ◽  
pp. 4768
Author(s):  
J E Ward ◽  
D E Akiyoshi ◽  
D Regier ◽  
A Datta ◽  
M P Gordon ◽  
...  

1987 ◽  
Vol 9 (6) ◽  
pp. 635-645 ◽  
Author(s):  
Leo S. Melchers ◽  
Dave V. Thompson ◽  
Ken B. Idler ◽  
Saskia T. C. Neuteboom ◽  
Ruud A. de Maagd ◽  
...  

1998 ◽  
Vol 11 (2) ◽  
pp. 131-143 ◽  
Author(s):  
Heenam Kim ◽  
Stephen K. Farrand

Opines are carbon compounds produced by crown galls and hairy roots induced by Agrobacterium tumefaciens and A. rhizogenes, respectively. These novel condensation products of plant metabolic intermediates are utilized as nutritional sources by the Agrobacterium strains that induced the growths. Thus, opines are thought to favor the propagation of agrobacteria in the tumorsphere. Certain Agrobacterium strains were chemoattracted to opines. The chemotactic activities to octopine, to nopaline, to manno-pine, and to agrocinopines A+B were dependent on the type of the Ti plasmid present in the bacterium. The determinants for chemotaxis to these opines were localized to the regions of the octopine- and nopaline-type Ti plasmids coding for transport and catabolism of that opine. An insertion in accA, which encodes the periplasmic binding protein for agrocinopines A+B, abolished chemotaxis while an insertion in accC, which encodes a component of the transport system, and an insertion in accF, which encodes a function required for agrocinopine catabolism, did not affect chemotaxis to this opine. Thus, transport and catabolism of these opines are not required for the chemo-tactic activity. Analyses of subclones of the acc region confirmed that accA is the only gene required from the Ti plasmid for chemotaxis to agrocinopines A+B.


1988 ◽  
Vol 11 (2) ◽  
pp. 227-237 ◽  
Author(s):  
Leo S. Melchers ◽  
Dave V. Thompson ◽  
Ken B. Idler ◽  
Saskia T. C. Neuteboom ◽  
Ruud A. de Maagd ◽  
...  

Microbiology ◽  
2005 ◽  
Vol 151 (11) ◽  
pp. 3483-3492 ◽  
Author(s):  
Paul K. Judd ◽  
David Mahli ◽  
Anath Das

The VirB proteins of Agrobacterium tumefaciens assemble a T-pilus and a type IV secretion (T4S) apparatus for the transfer of DNA and proteins to plant cells. VirB6 is essential for DNA transfer and is a polytopic integral membrane protein with at least four membrane-spanning domains. VirB6 is postulated to function in T-pilus biogenesis and to be a component of the T4S apparatus. To identify amino acids required for VirB6 function, random mutations were introduced into virB6, and mutants that failed to complement a deletion in virB6 in tumour formation assays were isolated. Twenty-one non-functional mutants were identified, eleven of which had a point mutation that led to a substitution in a single amino acid. Characterization of the mutants indicated that the N-terminal large periplasmic domain and the transmembrane domain TM3 are required for VirB6 function. TM3 has an unusual sequence feature in that it is rich in bulky hydrophobic amino acids. This feature is found conserved in the VirB6 family of proteins. Studies on the effect of VirB6 on other VirB proteins showed that the octopine Ti-plasmid VirB6, unlike its nopaline Ti-plasmid counterpart, does not affect accumulation of VirB3 and VirB5, but has a strong negative effect on the accumulation of the VirB7-VirB7 dimer. Using indirect immunofluorescence microscopy the authors recently demonstrated that VirB6 localizes to a cell pole in a VirB-dependent manner. Mutations identified in the present study did not affect polar localization of the protein or the formation of the VirB7-VirB7 dimer. A VirB6-GFP fusion that contained the entire VirB6 ORF did not localize to a cell pole in either the presence or the absence of the other VirB proteins. IMF studies using dual labelling demonstrated that VirB6 colocalizes with VirB3 and VirB9, and not with VirB4, VirB5 and VirB11. These results support the conclusion that VirB6 is a structural component of the T4S apparatus.


1988 ◽  
Vol 263 (12) ◽  
pp. 5804-5814
Author(s):  
J E Ward ◽  
D E Akiyoshi ◽  
D Regier ◽  
A Datta ◽  
M P Gordon ◽  
...  

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