scholarly journals Characterization of dull1, a Maize Gene Coding for a Novel Starch Synthase

1998 ◽  
Vol 10 (3) ◽  
pp. 399-412 ◽  
Author(s):  
Ming Gao ◽  
Jennifer Wanat ◽  
Philip S. Stinard ◽  
Martha G. James ◽  
Alan M. Myers
1998 ◽  
Vol 10 (3) ◽  
pp. 399 ◽  
Author(s):  
Ming Gao ◽  
Jennifer Wanat ◽  
Philip S. Stinard ◽  
Martha G. James ◽  
Alan M. Myers

1995 ◽  
Vol 8 (2) ◽  
pp. 283-294 ◽  
Author(s):  
Anne Edwards ◽  
Jacqueline Marshall ◽  
Christopher Sidebottom ◽  
Richard G.F. Visser ◽  
Alison M. Smith ◽  
...  

1992 ◽  
Vol 20 (15) ◽  
pp. 4092-4092 ◽  
Author(s):  
Hilla Giladi ◽  
Wei-Xian Wang ◽  
Amos B. Oppenheim

1998 ◽  
Vol 180 (20) ◽  
pp. 5285-5290 ◽  
Author(s):  
Richard van Kranenburg ◽  
Willem M. de Vos

ABSTRACT We characterized the regions involved in replication and mobilization of the 40-kb plasmid pNZ4000, encoding exopolysaccharide (EPS) production in Lactococcus lactis NIZO B40. The plasmid contains four highly conserved replication regions with homologous rep genes (repB1, repB2,repB3, and repB4) that belong to the lactococcal theta replicon family. Subcloning of each replicon individually showed that all are functional and compatible in L. lactis. Plasmid pNZ4000 and genetically labeled derivatives could be transferred to different L. lactis strains by conjugation, and pNZ4000 was shown to be a mobilization plasmid. Two regions involved in mobilization were identified near two of the replicons; both included an oriT sequence rich in inverted repeats. Conjugative mobilization of the nonmobilizable plasmid pNZ124 was promoted by either one of these oriT sequences, demonstrating their functionality. One oriT sequence was followed by a mobA gene, coding for atrans-acting protein, which increased the frequency of conjugative transfer 100-fold. The predicted MobA protein and theoriT sequences show protein and nucleotide similarity, respectively, with the relaxase and with the inverted repeat andnic site of the oriT from the Escherichia coli plasmid R64. The presence on pNZ4000 of four functional replicons, two oriT sequences, and several insertion sequence-like elements strongly suggests that this EPS plasmid is a naturally occurring cointegrate.


2001 ◽  
Vol 14 (4) ◽  
pp. 545-554 ◽  
Author(s):  
Gustavo Hernández-Guzmán ◽  
Ariel Alvarez-Morales

Pseudomonas syringae pv. phaseolicola is the causal agent of the “halo blight” disease of beans. A key component in the development of the disease is a nonhost-specific toxin, Nδ-(N'-sulphodiaminophosphinyl)-ornithyl-alanyl-homoarginine, known as phaseolotoxin. The homoarginine residue in this molecule has been suggested to be the product of Larginine:lysine amidinotransferase activity, previously detected in extracts of P. syringae pv. phaseolicola grown under conditions of phaseolotoxin production. We report the isolation and characterization of an amidinotransferase gene (amtA) from P. syringae pv. phaseolicola coding for a polypeptide of 362 residues (41.36 kDa) and showing approximately 40% sequence similarity to Larginine:inosamine-phosphate amidinotransferase from three species of Streptomyces spp. and 50.4% with an Larginine:glycine amidinotransferase from human mitochondria. The cysteine, histidine, and aspartic acid residues involved in substrate binding are conserved. Furthermore, expression of the amtA and argK genes and phaseolotoxin production occurs at 18°C but not at 28°C. An amidinotransferase insertion mutant was obtained that lost the capacity to synthesize homoarginine and phaseolotoxin. These results show that the amtA gene isolated is responsible for the amidinotransferase activity detected previously and that phaseolotoxin production depends upon the activity of this gene.


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