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Pumpkin phloem lectin genes are specifically expressed in companion cells. 1992

D E Bostwick, and J M Dannenhoffer, and M I Skaggs, and R M Lister, and B A Larkins, and G A Thompson
Department of Plant Sciences, University of Arizona, Tucson 85721.

Pumpkin phloem exudate contains two abundant phloem proteins: PP1 is a 96-kD protein that forms polymeric filaments in vivo, and PP2 is a 48-kD dimeric lectin. Polyclonal antibodies raised against pumpkin phloem exudate were used to isolate several cDNAs corresponding to PP1 and PP2. RNA gel blot analysis indicated that PP1 is encoded by an mRNA of approximately 2500 nucleotides, whereas PP2 subunits are encoded by an mRNA of 1000 nucleotides. Sequence analysis of PP2 cDNAs revealed a 654-bp open reading frame encoding a 218-amino acid polypeptide; this polypeptide had the carbohydrate binding characteristics of a PP2 subunit. The PP2 mRNA was localized within the phloem of pumpkin hypocotyl cross-sections based on in situ hybridization of a digoxigenin-labeled antisense probe. PP2 mRNA was found within the companion cells in both the bicollateral vascular bundles and the extrafascicular phloem network.

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
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
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
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
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D015870 Gene Expression The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION. Expression, Gene,Expressions, Gene,Gene Expressions
D017403 In Situ Hybridization A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes. Hybridization in Situ,Hybridization, In Situ,Hybridizations, In Situ,In Situ Hybridizations
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal
D037121 Plant Lectins Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms. Lectins, Plant,Phytagglutinin,Plant Agglutinin,Plant Lectin,Agglutinins, Plant,Phytagglutinins,Plant Agglutinins,Agglutinin, Plant,Lectin, Plant

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