The α2 cDNA sequence of human haptoglobin carries a bacterial promoter functional in vivo

1986 ◽  
Vol 6 (4) ◽  
pp. 363-373 ◽  
Author(s):  
Ariane van der Straten ◽  
Rosette Loriau ◽  
Albert Herzog ◽  
Alex Bollen
Keyword(s):  
Computer Analysis ◽  
Binding Sites ◽  
Cdna Sequence ◽  
Expression Vector ◽  
Β Subunit ◽  
Hybrid Protein ◽  
Ribosome Binding ◽  
Ribosome Binding Sites ◽  
Efficient Expression

Various constructions of human haptoglobin (Hp) cDNA coding either for the complete α2FSβ precursor protein or only for the β subunit have been placed under the control of the λPR promoter in the bacterial expression vector pCQV2 (Queen, 1983). In addition to the expected 45,000 dalton polypeptide synthesized after induction of the PR promoter, the complete α2FSβ constructions constitutively express a smaller polypeptide of ∼30,000 dalton corresponding to a truncated Hp protein. Computer analysis of the HpcDNA revealed the presence of two strong potential bacterial promoters (α2PF and α2PS) located in the duplicated α2FS sequence. Both Hp promoter signals are followed by potential mRNA start sites and ribosome binding sites at a compatible distance from initiation codons. In addition, the Hpα2 cDNA sequence, when fused upstream to the cDNA coding for α1-antitrypsin, constitutively promotes in vivo the efficient expression of an hybrid protein specifically recognized by antibodies raised against α1-antitrypsin or haptoglobin.

Design of Ribosome Binding Sites in Streptomyces coelicolor

2017 ◽  
Vol 14 (4) ◽  
Author(s):  
Hong-Dou Luo ◽  
Yang Tao ◽  
Wen-Guang Wang ◽  
Tao Lin ◽  
Yue-Yue Wang ◽  
...  
Keyword(s):  
Binding Sites ◽  
Streptomyces Coelicolor ◽  
Ribosome Binding ◽  
Ribosome Binding Sites

scholarly journals Tuning a bi-enzymatic cascade reaction in Escherichia coli to facilitate NADPH regeneration for ε-caprolactone production

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Jinghui Xiong ◽  
Hefeng Chen ◽  
Ran Liu ◽  
Hao Yu ◽  
Min Zhuo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Regeneration System ◽  
Nadph Regeneration ◽  
Whole Cell ◽  
Cyclohexanone Monooxygenase ◽  
Ribosome Binding ◽  
Ribosome Binding Sites ◽  
Whole Cell Biocatalyst ◽  
Substrate Tolerance

Abstractε-Caprolactone is a monomer of poly(ε-caprolactone) which has been widely used in tissue engineering due to its biodegradability and biocompatibility. To meet the massive demand for this monomer, an efficient whole-cell biocatalytic approach was constructed to boost the ε-caprolactone production using cyclohexanol as substrate. Combining an alcohol dehydrogenase (ADH) with a cyclohexanone monooxygenase (CHMO) in Escherichia coli, a self-sufficient NADPH-cofactor regeneration system was obtained. Furthermore, some improved variants with the better substrate tolerance and higher catalytic ability to ε-caprolactone production were designed by regulating the ribosome binding sites. The best mutant strain exhibited an ε-caprolactone yield of 0.80 mol/mol using 60 mM cyclohexanol as substrate, while the starting strain only got a conversion of 0.38 mol/mol when 20 mM cyclohexanol was supplemented. The engineered whole-cell biocatalyst was used in four sequential batches to achieve a production of 126 mM ε-caprolactone with a high molar yield of 0.78 mol/mol.

Expression of synthetic calcitonin genes in plasmid vectors containing tandemly repeated non-overlapping ribosome binding sites

1989 ◽  
Vol 21 (9) ◽  
pp. 987-996 ◽  
Author(s):  
Krassimir Alexciev ◽  
Anna Uscheva ◽  
Maja Pavlova ◽  
Libert Yavachev ◽  
Ivan Ivanov
Keyword(s):  
Binding Sites ◽  
Plasmid Vectors ◽  
Ribosome Binding ◽  
Ribosome Binding Sites

scholarly journals Evidence for Context-Dependent Complementarity of Non-Shine-Dalgarno Ribosome Binding Sites to Escherichia coli rRNA

2013 ◽  
Vol 8 (5) ◽  
pp. 958-966 ◽  
Author(s):  
Pamela A. Barendt ◽  
Najaf A. Shah ◽  
Gregory A. Barendt ◽  
Parth A. Kothari ◽  
Casim A. Sarkar
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Ribosome Binding ◽  
Ribosome Binding Sites ◽  
Context Dependent

scholarly journals Multiple divergent picobirnaviruses with functional prokaryotic Shine-Dalgarno ribosome binding sites present in cloacal sample of a diarrheic chicken

Virology ◽  
2018 ◽  
Vol 525 ◽  
pp. 62-72 ◽  
Author(s):  
Ákos Boros ◽  
Beáta Polgár ◽  
Péter Pankovics ◽  
Hajnalka Fenyvesi ◽  
Péter Engelmann ◽  
...  
Keyword(s):  
Binding Sites ◽  
Ribosome Binding ◽  
Ribosome Binding Sites

Quantitativer Vergleich der Initiator-Regionen (Ribosome Binding Sites) von 12 aus Escherichia coli stammenden Nukleotidsequenzen (RNA-und DNA-Phagen), die aus Triplets zusammengesetzt sind / Quantitative Comparison of Ribosome Binding Sites of Twelve Nucleotide Sequences from Escherichia coli (RNA-and DNA Phages) Based on Triplet Patterns

1979 ◽  
Vol 34 (9-10) ◽  
pp. 797-804 ◽  
Author(s):  
Erich Köhler
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Binary Sequence ◽  
Simple Calculation ◽  
Phage Gene ◽  
Ribosome Binding ◽  
Ribosome Binding Sites ◽  
Pyrimidine Bases ◽  
Triplet Code ◽  
Rna Phage

Abstract The molecular structure of ribosome binding sites of ten phage genes and two messengers of Escherichia coli were compared concerning the signation parts which are presumably used by ribosomes for recognition and binding. With a simple calculation based on triplet patterns sofar unknown agreements between all of these sequences were found. In several cases it was shown that agreements between old sequences are easier reognizable if the purine-and pyrimidine bases are put into the triplets instead of the four A, G, C, and U (T) bases. In such cases “homologous” parts of sequences were recognized with more distinctness. This is true in our case for the double triplet (hexaplet) py-pu-pu-pu-pu-(pu) and the binding site triplet py-pu-pu, which are preceding the ini­tiator. These triplets are in specific positions in all twelve sequences which were compared. The different course of the quaternary and the binary conformity curves (diagram 1) may show for the investigated area that the RNA phage gene-part is organized according to the well known quater­nary triplet code. On the contrary the phage φ-gene-part seems to be organized according to a more simple, binary triplet sequence of purine and pyrimidine bases. The binary sequence seems to be the more original, the quaternary the derived one.

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