Plant Glutamine Synthetase Complements a glnA Mutation in Escherichia coli
- 6 June 1986
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 232 (4755) , 1242-1244
- https://doi.org/10.1126/science.2871626
Abstract
A glutamine synthetase gene from alfalfa (Medicago sativa) has been expressed in Escherichia coli after fusion of bacterial transcription and translation signals to a complete alfalfa glutamine synthetase coding sequence. Synthesis of the alfalfa glutamine synthetase enzyme in Escherichia coli was demonstrated by functional genetic complementation of a glutamine synthetase-deficient mutant and by immunoblotting analysis. These results should facilitate protein engineering and structure-function analysis of the plant enzyme.This publication has 20 references indexed in Scilit:
- Lambda repressor mutations that increase the affinity and specificity of operator bindingCell, 1985
- Amino Acid Replacements that Compensate for a Large Polypeptide Deletion in an EnzymeScience, 1985
- Sites of allosteric shift in the structure of the cyclic AMP receptor proteinCell, 1985
- Assembly in E. coli of a functional multi-subunit ribulose bisphosphate carboxylase from a blue-green algaNature, 1985
- Heterogeneity of Glutamine Synthetase Polypeptides in Phaseolus vulgaris L.Plant Physiology, 1984
- GENETIC CONTROL OF NITROGEN ASSIMILATION IN BACTERIAAnnual Review of Genetics, 1982
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- A method for quantitative determination of cellular immunoglobulins by enzyme‐labeled antibodiesEuropean Journal of Immunology, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964