Disease relevance of araB

• We describe Escherichia coli survival following neutrophil phagocytosis among three mutants deleted respectively for araB, dps or oxyR [1].
• Here, we show that thermal induction of the prophage accelerated araB-lacZ fusion formation, confirming that derepression is a rate-limiting step in the fusion process [2].
• Bacteriophage M13 gene II has been cloned in the plasmid expression vector pING1 and thereby placed under the control of the inducible araB promoter of Salmonella typhimurium [3].
• Transaldolase/glucose-6-phosphate isomerase bifunctional enzyme and ribulokinase as factors to increase xylitol production from D-arabitol in Gluconobacter oxydans [4].

High impact information on araB

• Hybrid proteins formed by insertions in randomly selected genes and in the araB and A genes were examined by polyacrylamide gel electrophoresis [5].
• The results, when combined with the knowledge of the NH2-terminal sequence of the product of the first cistron (L-ribulokinase gene araB), establish the nucleotide sequence of the first 69 bases at the 5' end of the araBAD operon mRNA [6].
• Upon induction with arabinose, gene II is transcribed as part of a polycistronic messenger RNA which initiates at the araB promoter [3].
• The araB and araC genes of Salmonella typhimurium have been cloned onto the plasmid pBR322 [7].
• The nucleotide sequence of the araB promoter was 87% homologous with the same region in E. coli and contained no deletions or insertions relative to the E. coli sequence [7].

Chemical compound and disease context of araB

• High-Level Gene Expression for Recombinant Penicillin Acylase Production Using the araB Promoter System in Escherichia coli [8].

Biological context of araB

• Here we report that araA, araB and araD, whose inactivation leads to an Ara- phenotype, are the first three ORFs of a nine cistron transcriptional unit with a total length of 11 kb [9].

Associations of araB with chemical compounds

• The physiological and enzymatic properties of these L-arabinose non-utilizing mutants suggest that L-arabinose resistance is due to forward mutations in at least 3 other genes, araA, araB and araC, blocking steps prior to L-ribulose 5-phosphate accumulation [10].

References