Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1432-2242
    Keywords: Key words Phytochrome  ;  Tomato  ;  RFLPs  ;   Photomorphogenic mutants  ;  high pigment mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The map positions of five previously described phytochrome genes have been determined in tomato (Lycopersicon esculentum Mill.) The position of the yg-2 gene on chromosome 12 has been confirmed and the classical map revised. The position of the phytochrome A (phy A)-deficient fri mutants has been refined by revising the classical map of chromosome 10. The position of the PhyA gene is indistinguishable from that of the fri locus. The putative phyB1-deficient tri mutants were mapped by classical and RFLP analysis to chromosome 1. The PhyB1 gene, as predicted, was located at the same position. Several mutants with the high pigment (hp) phenotype, which exaggerates phytochrome responses, have been reported. Allelism tests confirmed that the hp-2 mutant is not allelic to other previously described hp (proposed here to be called hp-1) mutants and a second stronger hp-2 allele (hp-2 j ) was identified. The hp-2 gene was mapped to the classical, as well as the RFLP, map of chromosome 1.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1617-4623
    Keywords: Key words Photomorphogenic mutants ; Phytochrome ; Tomato ; PHYB2 ; Intron splicing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The structure of the gene encoding the apoprotein of tomato phytochrome B2 (PHYB2) has been determined from genomic and cDNA sequences. The coding region is organized into four exons, like almost every other angiosperm phytochrome (phy). The deduced phyB2 apoprotein (PHYB2) consists of 1121 amino acids, with 82, 74 and 70% identity to tomato PHYB1, Arabidopsis PHYB, and Arabidopsis PHYD, respectively. In order to facilitate the identification of new mutants, we constructed a double mutant that is deficient in phyA and phyB1. When grown in white light, this mutant becomes only slightly taller than wild type and is similar in phenotype to the monogenic phyB1-deficient mutant. This double mutant has been used as the parent line for mutagenesis with γ radiation. Several recessive mutants with long hypocotyls and reduced anthocyanin content were selected under white light and screened for mutations in PHYB2, PHYE and PHYF. Two of the triple-mutant lines, designated 55H and 70F, had elongated hypocotyls and fruit trusses, and pale immature fruits. Both belong to the same complementation group and both were found to have defects in PHYB2. Line 70F was found by Northern analysis to have a slightly larger PHYB2 transcript. Part or all of the intron between the second and third exons was found to be retained following RT-PCR of PHYB2 mRNA from line 70F. Three base substitutions were detected near the donor splice site for this intron, including a change from the consensus /GT to /GA at the 5′ end of this intron. In every case, the C-terminal 164 amino acids of PHYB2 were replaced by 59 nonsense amino acids followed by a stop codon. Sequencing of PHYB2 from 55H revealed a single-nucleotide deletion near the end of the third exon, resulting in one incorrect codon followed immediately by a stop codon. The predicted mutant apoprotein in 55H is 90 residues shorter than wild-type PHYB2.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Phytochrome apoproteins in angiosperms are encoded by a small gene family. Tomato (Solatium lycopersicum L.) serves well as a dicotyledonous model system for elucidating the extent of this gene family, its expression patterns, and the roles of individual members of the family. Five phytochrome genes (PHYA, PHYB1, PHYB2, PHYE and PHYF have been characterized in tomato. Quantitative measurements of transcript abundances from each tomato PHY throughout the life cycle indicate that transcript levels generally range from 10 to 100 μmol mol−1 total mRNA, in the following order of decreasing abundance: PHYA, PHYB1, PHYE, PHYB2 and PHYF. PHYA transcripts were found to be most abundant in seedling roots, while PHYB2 and PHYF transcripts were expressed preferentially in fruit. PHYA mutants (fri) have been found to be the consequence of a single nucleotide substitution adjacent to the 3′ terminus of an intron. What are almost certainly PHYB1 mutants have also been described, although the molecular nature of these mutants remains to be revealed. Efforts to obtain PHYB2, PHYE and PHYF mutants are currently underway.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1432-2048
    Keywords: Avena (phytochrome) ; Enzyme-linked immunosorbent assay (ELISA) ; Immunoprecipitation ; Monoclonal antibody ; Phytochrome from green and etiolated tissue ; Pisum (phytochrome)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract While two monoclonal antibodies directed to phytochrome from etiolated oat (Avena sativa L.) shoots can precipitate up to about 30% of the photoreversible phytochrome isolated from green oat shoots, most precipitate little or none at all. These results are consistent with a report by J.G. Tokuhisa and P.H. Quail (1983, Plant Physiol. 72, Suppl., 85), according to which polyclonal rabbit antibodies directed to phytochrome from etiolated oat shoots bind only a small fraction of the phytochrome obtained from green oat shoots. The immunoprecipitation data reported here indicate that essentially all phytochrome isolated from green oat shoots is distinct from that obtained from etiolated oat shoots. The data indicate further that phytochrome from green oat shoots might itself be composed of two or more immunochemically distinct populations, each of which is distinct from phytochrome from etiolated shoots. Phytochrome isolated from light-grown, but norflurazon-bleached oat shoots is like that isolated from green oat shoots. When light-grown, green oat seedlings are kept in darkness for 48 h, however, much, if not all, of the phytochrome that reaccumulates is like that from etiolated oat shoots. Neither modification during purification from green oat shoots of phytochrome like that from etiolated oat shoots, nor non-specific interference by substances in extracts of green oat shoots, can explain the inability of antibodies to recognize phytochrome isolated from green oat shoots. Immunopurified polyclonal rabbit antibodies to phytochrome from etiolated pea (Pisum sativum L.). shoots precipitate more than 95% of the photoreversible phytochrome obtained from etiolated pea shoots, while no more than 75% of the pigment is precipitated when phytochrome is isolated from green pea shoots. These data indicate in preliminary fashion that an immunochemically unique pool of phytochrome might also be present in extracts of green pea shoots.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 1432-2048
    Keywords: Avena (phytochrome) ; Monoclonal antibodies (phytochrome) ; Phytochrome (sequestering)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The kinetics of the intracellular redistribution of phytochrome (sequestering) in Avena sativa L. coleoptiles following a brief, saturating actinic pulse of red (R) light have been determined. Immunocytochemical labelling of phytochrome with monoclonal antibodies showed that at 22°C sequestering can occur within 1–2 s from the onset of R irradiation and is dependent upon the continued presence of the far-red-absorbing form of phytochrome (Pfr). The initial rate, but not the final extent, of sequestering is reduced by lowering the temperature of the tissue to 1°C. Sequestering at 22°C appears to involve two distinct stages: (1) a rapid association of Pfr with putative binding sites initiates the sequestered condition, following which (2) these sites of sequestered phytochrome appear to aggregate. Neither of these two processes was affected by the cytoskeletal inhibitors colchicine or cytochalasin B. Phytochrome sequestering therefore resembles R-light-induced phytochrome pelletability with respect to kinetics, temperature sensitivity, and dependence upon the continued presence of Pfr in the cell.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 1432-2048
    Keywords: Phytochrome ; Lycopersicon ; Photomorphogenic mutants ; Photomorphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four monogenic recessive tomato (Lycopersicon esculentum Mill.) mutants at the temporarily red light-Insensitive (tri) locus (tri 1, tri 2in the genetic background breeding line GT; tri 3, tri 4in the genetic background cultivar Moneymaker) were studied. These mutants had slightly longer hypocotyls under white light than the wild type (WT). Western-blot analysis showed that the tri 1mutant was deficient in a relatively lightstable phytochrome apoprotein (116 kDa) that was recognized in the WT by an antibody to tobacco phytochrome B; tri 2had a 166-kDa band reduced in abundance; and tri 2and tri 4had bands reduced in molecular mass, approx. 105 and 95 kDa, respectively. These patterns were also found in light-grown plants. Northern-blot analysis for PHYB1 mRNA showed for tri 2a transcript approx. 2 kb larger, for tri 4, a transcript of WT size, but much reduced in abundance and for tri 1and tri 3transcripts equivalent in size and abundance to WT. In these mutants the transcripts of other members of the tomato phytochrome gene family (PHYA, PHYB2, PHYE, PHYF) were indistinguishable in size and abundance from WT. Thus, it appears that the tri locus specifically affects PHYB1 gene expression. Unlike phytochrome-B mutants in other plants, de-etiolated seedlings of the tri mutants exhibited normal responses to end-of-day far-red (EODFR) light and supplementary far-red light during the day. Since the holophytochromes of types B1 and B2 (phyB1 and phyB2) are closely related, it is proposed that there might be redundancy between them for these responses.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 1432-2048
    Keywords: Avena (phytochrome) ; Phytochrome from green and etiolated tissue
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thirty-nine antiserum preparations from eight rabbits were screened for their ability to precipitate the immunochemically distinct phytochrome that is obtained from green oat (Avena sativa L.) shoots. The antisera were obtained from rabbits immunized with either proteolytically degraded, but still photoreversible, 60-kDa (kilodalton) phytochrome, or approx. 120-kDa phytochrome, both of which were purified from etiolated oat shoots. The ability of these antisera to precipitate phytochrome from green oats was independent of the size of phytochrome used for immunization. While crude antisera immunoprecipitated as much as 80% of the phytochrome isolated from green oat shoots, antibodies immunopurified from these sera with a column of highly purified, approx. 120-kDa phytochrome from etiolated oats precipitated no more than about 5–10%.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 8
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary PIDDLE is a cloning strategy coupling antibody techniques to PCR. Degenerate, multifunctional header-primers derived from peptide data prime a single- or double-step PCR on genomic or cDNA template. Terminal restriction sites are thereby created to allow efficient, in-frame, directional cloning into the pBluescript-like pIDDLE phagemid. A chimeric protein is then expressed in E.coli and recognised by antibodies to the native protein. PIDDLE may also be used to generate antibodies. We describe PIDDLE cloning of phy from oat.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 33 (1982), S. 557-582 
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...