Differential expression in Escherichia coli of the alpha and beta forms of heparin-binding acidic fibroblast growth factor-1: potential role of RNA secondary structure
| Autor: | Reza Forough, John A. Thompson, Toru Imamura, Kurt Engleka, Thomas Maciag, Anthony Jackson |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
DNA
Bacterial Molecular Sequence Data Biophysics Alpha (ethology) Biology medicine.disease_cause Biochemistry Nucleic acid secondary structure Eukaryotic translation Structural Biology Genetics medicine Escherichia coli Cloning Molecular Beta (finance) Polymerase Expression vector Base Sequence Translation (biology) Gene Expression Regulation Bacterial Molecular biology RNA Bacterial Protein Biosynthesis biology.protein Fibroblast Growth Factor 1 Nucleic Acid Conformation RNA |
| Zdroj: | Biochimica et biophysica acta. 1090(3) |
| ISSN: | 0006-3002 |
| Popis: | Synthetic DNA fragments encoding the entire open-reading frame of human heparin-binding growth factor-1 (HBGF-1 beta) and its NH2-terminal truncated form (HBGF-1 alpha) were constructed. When both constructs were expressed in Escherichia coli under control of the trp-lac promoter, biologically active HBGF-1 alpha, but not HBGF-1 beta was produced in high yield. However, high level expression of HBGF-1 beta was obtained using the T7 polymerase expression vector. Computer analysis of HBGF-1 beta predicts the potential for the formation of exaggerated RNA secondary structure near the translation initiation codon and this could be implicated in contributing to the poor translation of HBGF-1 beta under the trp-lac promoter. |
| Databáze: | OpenAIRE |
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