The bacterial phleomycin resistance gene ble as a dominant selectable marker in Chlamydomonas. 1996

D R Stevens, and J D Rochaix, and S Purton
Department of Biology, University College London, UK.

A chimeric gene composed of the coding sequence of the ble gene from Streptoalloteichus hindustanus fused to the 5' and 3' untranslated regions of the Chlamydomonas reinhardtii nuclear gene RBCS2 has been constructed. Introduction of this chimeric gene into the nuclear genome of C. reinhardtii by co-transformation with the ARG7 marker yields Arg+ transformants of which approximately 80% possess the ble gene. Of these co-transformants, approximately 3% display a phleomycin-resistant (PmR) phenotype. Western blot analysis using antibodies against the ble gene product confirms the presence of the protein in the PmR transformants and genetic analysis demonstrates the co-segregation of the ble gene with the phenotype in progeny arising from the mating of a PmR transformant to wild-type strains. Direct selection of PmR transformants was achieved by allowing an 18-h period for recovery and growth of transformed cells prior to selection. This work represents the first demonstration of stable expression and inheritance of a foreign gene in the nuclear genome of C. reinhardtii and provides a useful dominant marker for nuclear transformation.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010641 Phenotype The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment. Phenotypes
D010692 Phleomycins Water-soluble, copper-containing low molecular weight polypeptides obtained from the culture medium of Streptomyces verticillus. They are specific inhibitors of DNA synthesis in bacteria and have been found to act as antitumor agents. They have also been used against rust fungi of plants. Phleomycin
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
D004352 Drug Resistance, Microbial The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS). Antibiotic Resistance,Antibiotic Resistance, Microbial,Antimicrobial Resistance, Drug,Antimicrobial Drug Resistance,Antimicrobial Drug Resistances,Antimicrobial Resistances, Drug,Drug Antimicrobial Resistance,Drug Antimicrobial Resistances,Drug Resistances, Microbial,Resistance, Antibiotic,Resistance, Drug Antimicrobial,Resistances, Drug Antimicrobial
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D012273 Ribulose-Bisphosphate Carboxylase A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration. Carboxydismutase,Ribulose Biphosphate Carboxylase-Oxygenase,Ribulose Diphosphate Carboxylase,Ribulosebiphosphate Carboxylase,Rubisco,1,5-Biphosphate Carboxylase-Oxygenase,Ribulose Biphosphate Carboxylase,Ribulose Bisphosphate Carboxylase,Ribulose-1,5-Biphosphate Carboxylase,Ribulose-1,5-Biphosphate Carboxylase-Oxygenase,Ribulose-1,5-Bisphosphate Carboxylase Small-Subunit,Ribulose-Bisphosphate Carboxylase Large Subunit,Ribulose-Bisphosphate Carboxylase Small Subunit,Rubisco Small Subunit,1,5 Biphosphate Carboxylase Oxygenase,Biphosphate Carboxylase-Oxygenase, Ribulose,Carboxylase Small-Subunit, Ribulose-1,5-Bisphosphate,Carboxylase, Ribulose Bisphosphate,Carboxylase, Ribulose Diphosphate,Carboxylase, Ribulose-1,5-Biphosphate,Carboxylase, Ribulose-Bisphosphate,Carboxylase, Ribulosebiphosphate,Carboxylase-Oxygenase, 1,5-Biphosphate,Carboxylase-Oxygenase, Ribulose Biphosphate,Carboxylase-Oxygenase, Ribulose-1,5-Biphosphate,Diphosphate Carboxylase, Ribulose,Ribulose 1,5 Biphosphate Carboxylase,Ribulose 1,5 Biphosphate Carboxylase Oxygenase,Ribulose 1,5 Bisphosphate Carboxylase Small Subunit,Ribulose Biphosphate Carboxylase Oxygenase,Ribulose Bisphosphate Carboxylase Large Subunit,Ribulose Bisphosphate Carboxylase Small Subunit,Small Subunit, Rubisco,Small-Subunit, Ribulose-1,5-Bisphosphate Carboxylase

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