Biomaterial Database

Targeted inactivation of the gene psaK encoding a subunit of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803. 1999

H Nakamoto, and M Hasegawa

Department of Biochemistry and Molecular Biology, Saitama University, Urawa, Japan. nakamoto@sacs.sv.saitama-u.ac.jp

Mutant strains of the unicellular cyanobacterium Synechocystis sp. PCC 6803, in which the psaK gene was insertionally inactivated by targeted mutagenesis, were constructed. The gene is one of the two potential PsaK-coding genes which have been found as a result of the genome project with this cyanobacterium. One of the mutants was characterized in detail. A monocistronic, 480-nucleotide mRNA of psaK was absent in total RNA from the mutant cells. Inactivation of psaK had little effect on the accumulation of polypeptides in the isolated PSI complexes except for a polypeptide with an apparent molecular mass of 4.6 kDa which was absent in the mutant. The amino-terminal amino acid sequence of the 4.6-kDa polypeptide confirmed that it was the translation product of psaK and further revealed a presequence of PsaK. Characteristics of photoautotrophic growth at different temperatures, the amount of chlorophyll per cell, photosynthetic electron transport rates with rates with various electron acceptors, the kinetics of charge recombination between P700+ and reduced FA/FB, and the molar ratio of chlorophyll to P700, of the mutant were not significantly different from those of the wild type. Furthermore, the trimer to monomer ratio of the PSI complexes isolated from the mutant was similar to that isolated from the wild type.

UI	MeSH Term	Description	Entries
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
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
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D010788	Photosynthesis	The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)	Calvin Cycle,Calvin-Benson Cycle,Calvin-Benson-Bassham Cycle,Carbon Fixation, Photosynthetic,Reductive Pentose Phosphate Cycle,Dark Reactions of Photosynthesis,Calvin Benson Bassham Cycle,Calvin Benson Cycle,Cycle, Calvin,Cycle, Calvin-Benson,Cycle, Calvin-Benson-Bassham,Photosynthesis Dark Reaction,Photosynthesis Dark Reactions,Photosynthetic Carbon Fixation
D011498	Protein Precursors		Precursors, Protein
D002734	Chlorophyll	Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.	Phyllobilins,Chlorophyll 740
D004579	Electron Transport	The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)	Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D005798	Genes, Bacterial	The functional hereditary units of BACTERIA.	Bacterial Gene,Bacterial Genes,Gene, Bacterial
D000458	Cyanobacteria	A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.	Algae, Blue-Green,Blue-Green Bacteria,Cyanophyceae,Algae, Blue Green,Bacteria, Blue Green,Bacteria, Blue-Green,Blue Green Algae,Blue Green Bacteria,Blue-Green Algae
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein