Disease relevance of chiA

• In contrast, CBD2 and CBD3 were classified into that of the family II type. chiA was expressed in Escherichia coli cells, and the recombinant protein was purified to homogeneity [1].
• The chiA gene from Aeromonas caviae encodes an extracellular chitinase, 865 amino acids long, that shows a high degree of similarity to chitinase A of Serratia marcescens [2].
• The partial open reading frame (chiA) downstream from pfp was similar to chitinase genes from Streptomyces species [3].
• Cloning and primary structure of the chiA gene from Aeromonas caviae [2].
• A family 18 chitinase gene chiA from the thermophile Rhodothermus marinus was cloned and expressed in Escherichia coli [4].

High impact information on chiA

• The gene cluster consisted of three different open reading frames organized in the order chiD, cbp1, and chiA [5].
• The region upstream of chiA included a conserved -35 hexamer flanked by two direct repeats analogous to those found in many Streptomyces chitinase promoters, and thought to function as binding sequences for regulatory proteins [6].
• The gene ensemble consists of 4CL-2 (4-coumarate:CoA ligase) and FSI (flavone synthase I) from parsley, chsA (chalcone synthase) and chiA (chalcone isomerase) from Petunia hybrida, and OMT1A (7-O-methyltransferase) from peppermint [7].
• A protein purification procedure was developed to efficiently and effectively purify the target enzyme, chitinase A1 of Bacillus circulans WL-12, from Escherichia coli DH5alpha carrying the chiA gene with its natural promoter in the plasmid pNTU110 [8].
• The chitinase gene product showed amino-acid sequence similarity to chiA from A. caviae [9].

Biological context of chiA

• A gene cluster involved in the chitinolytic system of the strain was cloned and sequenced upstream of and including the chiA gene [5].
• Primer-extension analysis confirmed that the transcription of this operon starts upstream of chiA [10].
• The nucleotide sequence of the chiA gene from Serratia marcescens strain BJL200 was determined [11].
• A protein that binds specifically to the promoter region of chiA was purified from the cell lysate of Streptomyces lividans by using an affinity purification method [12].
• Chitinbiose was produced at more than 4 g L-1 by a high cell density culture of an Escherichia coli strain that co-expressed the rhizobial chitinoligosaccharide synthase gene nodC and a truncated form of the chitinase gene chiA which has been designed to be functionally produced in the E. coli cytoplasm [13].

Anatomical context of chiA

• ChiA was purified from the periplasm fraction of Escherichia coli harboring the chiA gene [10].

Associations of chiA with chemical compounds

• The gene-specific PCR primers were used to detect the presence of the chiA gene in strain C4 [14].

Other interactions of chiA

• Expression of chiA was investigated using Escherichia coli beta-galactosidase as a reporter enzyme [15].

Analytical, diagnostic and therapeutic context of chiA

• The modified chiA genes were expressed in Escherichia coli, and the gene products were analyzed after purification by high-performance liquid chromatography [16].
• Northern blot analysis indicated that the chiA and chiB genes constitute a polycistronic operon [10].

References