BIOMAT Database Logo BIOMAT Database Logo

The genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase are expressed differentially in petunia leaves. 1986

N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah

We have isolated five members of the multigene family encoding the small subunit (rbcS) of ribulose-1,5-bisphosphate carboxylase in petunia and examined their expression in petunia leaves. Of the five rbcS genes, two (ssu11A and ssu8) are expressed at high levels in petunia leaves. Northern analysis using gene specific oligonucleotide probes revealed that ssu11A accounts for 40% of the total rbcS transcripts in petunia leaves while ssu8 accounts for 4 to 5% of the total rbcS transcripts. Structural comparisons of ssu8 and ssu11A revealed that the coding sequence of ssu8 is interrupted by three introns, while the coding sequence of ssu11A is interrupted by two introns. The positions of the first two introns are identical, the third intron in ssu8 is located in a highly conserved region of the protein. The 5' and 3' flanking sequences of ssu11A are highly homologous to the 5' and 3' flanking sequences of ssu8. S1 nuclease mapping was used to locate the start of transcription of ssu8 and ssu11A and showed that ssu8 mRNA leader differs in sequence from the ssu11A mRNA leader.

UI MeSH Term Description Entries
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004262 DNA Restriction Enzymes Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1. Restriction Endonucleases,DNA Restriction Enzyme,Restriction Endonuclease,Endonuclease, Restriction,Endonucleases, Restriction,Enzymes, DNA Restriction,Restriction Enzyme, DNA,Restriction Enzymes, DNA
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
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
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
D014158 Transcription, Genetic The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION. Genetic Transcription
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Small subunit contacts in ribulose-1,5-bisphosphate carboxylase.
February 1978, Biochemistry,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Degradation products of the mRNA encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in soybean and transgenic petunia.
January 1992, The Plant cell,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Differential expression of individual genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in Lemna gibba.
July 1990, Plant molecular biology,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Role of the small subunit in ribulose-1,5-bisphosphate carboxylase/oxygenase.
June 2003, Archives of biochemistry and biophysics,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
The gene family encoding the ribulose-(1,5)-bisphosphate carboxylase/oxygenase (Rubisco) small subunit of potato.
December 1993, Gene,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Nucleotide sequence and molecular evolution of two tomato genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase.
January 1986, Gene,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Nucleotide sequence of cDNA encoding the small subunit of ribulose-1,5-bisphosphate carboxylase from maize.
October 1987, Journal of biochemistry,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Monomeric behavior of the small subunit of ribulose-1,5-bisphosphate carboxylase.
June 1976, Biochemical and biophysical research communications,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Photoregulation of expression of genes encoding ribulose-1,5-bisphosphate carboxylase/oxygenase.
February 1986, Biochemical Society transactions,
N E Tumer, and W G Clark, and G J Tabor, and C M Hironaka, and R T Fraley, and D M Shah
Nucleotide sequence of a gene encoding sunflower ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit (rbcs).
September 1987, Nucleic acids research,
Copied contents to your clipboard!