TheglgBgene from the thermophileBacillus caldolyticusencodes a thermolabile branching enzyme
| Autor: | Gerhardus Venema, J. A. K. W. Kiel, J. M. Boels, G. Beldman |
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| Rok vydání: | 1992 |
| Předmět: |
DNA
Bacterial Molecular Sequence Data Restriction Mapping Gene Expression Bacillus Bacillus subtilis Biology Biochemistry Open Reading Frames chemistry.chemical_compound Endocrinology Sigma factor 1 4-alpha-Glucan Branching Enzyme RNA polymerase Enzyme Stability Escherichia coli Genes Overlapping Genetics Glycogen branching enzyme Amino Acid Sequence Cloning Molecular Thermolabile Codon Molecular Biology Gene Base Composition Base Sequence Sequence Homology Amino Acid fungi Structural gene Temperature biology.organism_classification Open reading frame chemistry Genes Bacterial biology.protein bacteria Plasmids |
| Zdroj: | DNA Sequence. 3:221-232 |
| ISSN: | 1042-5179 |
| DOI: | 10.3109/10425179209034021 |
| Popis: | We have cloned the structural gene for the Bacillus caldolyticus glycogen branching enzyme (glgB) in Escherichia coli. The glgB gene consisted of a 1998 bp open reading frame (ORF) encoding a 78,087 Da protein, which was highly similar to the Bacillus stearothermophilus branching enzyme. The 5' end of a second gene that encoded a protein with extensive similarity to E. coli ADP-glucose pyrophosphorylase (ADPGP) partly overlapped the 3' end of the glgB gene. A putative promoter recognized by Bacillus subtilis RNA polymerase containing the sigma factor H (E-sigma H) preceded the genes. These data suggest that in contrast to the situation observed in B. stearothermophilus, the genes involved in glycogen synthesis in B. caldolyticus are clustered on the chromosome, and are presumably coordinately expressed during the early stages of sporulation. An incomplete third gene started upstream of B. caldolyticus glgB. This gene was highly similar to a gene found directly upstream of B. stearothermophilus glgB, which encodes a putative membrane protein with unknown function. The B. caldolyticus glgB gene was expressed in E. coli and B. subtilis. Surprisingly, the branching enzyme appeared to be thermolabile, the temperature of optimal activity being only 39 degrees C. |
| Databáze: | OpenAIRE |
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