Molecular Characterization of Barley Methionine γ-Lyase and Gene Expression by Abiotic Stress and Aspartate Family Amino Acids

2017 ◽  
Vol 05 (03) ◽  
Author(s):  
Manabu Sugimoto ◽  
Hidehiko Tanaka ◽  
Nobutada Murakami
2011 ◽  
Vol 5 (5) ◽  
pp. e1167 ◽  
Author(s):  
Rubens L. do Monte-Neto ◽  
Adriano C. Coelho ◽  
Frédéric Raymond ◽  
Danielle Légaré ◽  
Jacques Corbeil ◽  
...  

Hydrobiologia ◽  
2005 ◽  
Vol 546 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Gen Kaneko ◽  
Tatsuki Yoshinaga ◽  
Yoshiko Yanagawa ◽  
Shigeharu Kinoshita ◽  
Katsumi Tsukamoto ◽  
...  

1990 ◽  
Vol 45 (5) ◽  
pp. 538-543 ◽  
Author(s):  
D. Friedberg ◽  
J. Seijffers

We present here the isolation and molecular characterization of acetolactate synthase (ALS) genes from the cyanobacterium Synechococcus PCC7942 which specify a sulfonylurea-sensitive enzyme and from the sulfonylurea-resistant mutant SM3/20, which specify resistance to sulfonylurea herbicides. The ALS gene was cloned and mapped by complementation of an Escherichia coli ilv auxotroph that requires branched-chain amino acids for growth and lacks ALS activity. The cyanobacterial gene is efficiently expressed in this heterologous host. The ALS gene codes for 612 amino acids and shows high sequence homology (46%) at the amino acid level with ALS III of E. coli and with the tobacco ALS. The resistant phenotype is a consequence of proline to serine substitution in residue 115 of the deduced amino acid sequence. Functional expression of the mutant gene in wild-type Synechococcus and in E. coli confirmed that this amino-acid substitution is responsible for the resistance. Yet the deduced amino-acid sequence as compared with othjer ALS proteins supports the notion that the amino-acid context of the substitution is important for the resistance.


2006 ◽  
Vol 119 (1) ◽  
pp. 91-98 ◽  
Author(s):  
Angel Chao ◽  
Tzu-Hao Wang ◽  
Yun-Shien Lee ◽  
Swei Hsueh ◽  
An-Shine Chao ◽  
...  

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