BIOMAT Database Logo BIOMAT Database Logo

The oligopeptide (Gly-Pro)2-Ala-(Gly-Pro)2 increases the internal proline level and improves NaCl tolerance when produced in Escherichia coli. 1991

L Bülow, and K Mosbach
Department of Pure and Applied Biochemistry, Chemical Center, Lund, Sweden.

We have produced various proline-containing peptides as translational fusions with beta-glucuronidase (beta Glu) in Escherichia coli. When these linkers were introduced in the 5'-end of the beta Glu-encoding gene, the production of the enzyme was increased substantially in vivo. The peptides carrying repetitive Gly-Pro sequences could also stimulate the growth of the transformants in media with inhibitory concentrations of NaCl. Furthermore, the freezing tolerance could be improved.

UI MeSH Term Description Entries
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D011392 Proline A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons. L-Proline,L Proline
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005615 Freezing Liquids transforming into solids by the removal of heat. Melting
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D005966 Glucuronidase Endo-beta-D-Glucuronidase,Endoglucuronidase,Exo-beta-D-Glucuronidase,beta-Glucuronidase,Endo beta D Glucuronidase,Exo beta D Glucuronidase,beta Glucuronidase
D012965 Sodium Chloride A ubiquitous sodium salt that is commonly used to season food. Sodium Chloride, (22)Na,Sodium Chloride, (24)NaCl
D014170 Transformation, Genetic Change brought about to an organisms genetic composition by unidirectional transfer (TRANSFECTION; TRANSDUCTION, GENETIC; CONJUGATION, GENETIC, etc.) and incorporation of foreign DNA into prokaryotic or eukaryotic cells by recombination of part or all of that DNA into the cell's genome. Genetic Transformation,Genetic Transformations,Transformations, Genetic
D014882 Water-Electrolyte Balance The balance of fluid in the BODY FLUID COMPARTMENTS; total BODY WATER; BLOOD VOLUME; EXTRACELLULAR SPACE; INTRACELLULAR SPACE, maintained by processes in the body that regulate the intake and excretion of WATER and ELECTROLYTES, particularly SODIUM and POTASSIUM. Fluid Balance,Electrolyte Balance,Balance, Electrolyte,Balance, Fluid,Balance, Water-Electrolyte,Water Electrolyte Balance

Related Publications

L Bülow, and K Mosbach
Oligopeptides with the sequences ala-pro-gly and gly-pro-gly as substrates or inhibitors for protocollagen proline hydroxylase.
May 1969, The Journal of biological chemistry,
L Bülow, and K Mosbach
Collagenase action on the synthetic tripeptide polymers, (gly-pro-ala)n and (gly-ala-pro)n.
July 1969, Biochimica et biophysica acta,
L Bülow, and K Mosbach
Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices.
July 2001, The Journal of biological chemistry,
L Bülow, and K Mosbach
Conformational change of the triple-helical structure. II. Conformation of (Pro-Pro-Gly)n and (Pro-Pro-Gly)n (Ala-Pro-Gly)m(Pro-Pro-Pro-Gly)n in an aqueous solution.
November 1974, Biopolymers,
L Bülow, and K Mosbach
Coacervation properties in sequential polypeptide models of elastin. Synthesis of H-(Ala-Pro-Gly-Gly)n-Val-OMe and H-(Ala-Pro-Gly-Val-Gly)n-Val-OMe.
August 1978, International journal of peptide and protein research,
L Bülow, and K Mosbach
Cooperative stabilization of Escherichia coli ribonuclease HI by insertion of Gly-80b and Gly-77-->Ala substitution.
July 1993, Biochemistry,
L Bülow, and K Mosbach
[Effects of dipeptides Gly-Pro, Pro-Gly, glycine, and proline on the cardiotropic effect of acetylcholine].
August 1998, Biulleten' eksperimental'noi biologii i meditsiny,
L Bülow, and K Mosbach
Structural and morphological investigation of poly (gly-ala-pro).
April 1970, Nature,
L Bülow, and K Mosbach
Solution conformations of two flexible cyclic pentapeptides: cyclo(Gly-Pro-D-Phe-Gly-Ala) and cyclo(Gly-Pro-D-Phe-Gly-Val).
December 1992, Biopolymers,
L Bülow, and K Mosbach
Conversion of the amino acid sequence gly-pro-pro in protein to gly-pro-hyp by collagen proline hydroxylase.
August 1967, Archives of biochemistry and biophysics,
Copied contents to your clipboard!