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  • 1
    Electronic Resource
    Electronic Resource
    Subunit interactions in the carboxy-terminal domain of phytochrome (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 8239-8245 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00083a026
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  • 2
    Electronic Resource
    Electronic Resource
    Quaternary structure of 124-kilodalton phytochrome from Avena sativa L (1986)
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 2987-2995 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00358a038
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  • 3
    Electronic Resource
    Electronic Resource
    The Learning Organization: Adult Learning and Organizational Transformation (1994)
    Oxford, UK : Blackwell Publishing Ltd
    British journal of management 5 (1994), S. 0 
    Details
    ISSN: 1467-8551
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Economics
    Notes: The concept of the ‘learning organization’, with its roots in self-development and action-learning, has recently caught the imagination of many organizations and researchers. However, emerging definitions are creating ambiguity. There is, therefore, a need to add substance to them, and widen our understanding of what the concept means, by concentrating on what is meant by ‘learning’, and focusing on exactly how adults learn. Understanding and facilitating adult learning in organizations is, by and large, a confused activity that fails to connect with an individual's other experiences and needs, and with what modern psychology and research have to teach us. In particular, learning and skills need to be linked to the questioning of purpose and value in an organization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1467-8551.1994.tb00075.x
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  • 4
    Electronic Resource
    Electronic Resource
    Do we have the auxin receptor yet? (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 80 (1990), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Several auxin-binding proteins (ABP) have now been identified using a variety of techniques. A 43-kDa glycoprotein thought to be a dimer of 22-kDa subunits has been identified as a strong candidate for the auxin receptor that mediates cell elongation in etiolated maize shoots. The primary sequence has been deduced and several interesting structural features have been discerned. There is indirect evidence that this 22-kDa ABP has a receptor function, the most compelling being that antibodies directed against the ABP can block an auxin-induced response. There is evidence that changes in auxin-induced growth capacity in shoots correlates with changes in the abundance of the 22-kDa ABP suggesting that in some cases the 22-kDa ABP may be limiting growth. Confirmation of receptor function for one of these newly-identified ABP's should open the way for genetic manipulation of crop growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1990.tb04390.x
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  • 5
    Electronic Resource
    Electronic Resource
    Phytochrome-mediated swelling of etiolated leaf protoplasts and its possible biological significance (1990)
    Springer
    Plant cell reports 9 (1990), S. 435-438 
    Details
    ISSN: 1432-203X
    Keywords: Phytochrome-Pisum ; sativum-Protoplasts-(Protoplast) ; Swelling-(Leaf) Unrolling-Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Red light, mediated by the photoreceptor phytochrome, induces maize leaf unrolling as well as leaf expansion. Protoplasts prepared from maize leaves still in the rolled condition swell in a red-far red photoreversible manner indicating that phytochrome mediates this phenomenon. To determine if protoplast swelling is related to leaf unrolling, leaf expansion, or both, we compared red-light induced swelling of protoplasts from rolled maize leaves to protoplasts prepared from tissues that are known to grow in response to light but do not unroll. We also compared the swelling response of protoplasts from rolled vs. unrolled leaves. In all cases, we found that swelling correlated with the unrolling response and not leaf expansion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232267
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  • 6
    Electronic Resource
    Electronic Resource
    Comparison of Site I auxin binding and a 22-kilodalton auxin-binding protein in maize (1989)
    Springer
    Planta 179 (1989), S. 409-413 
    Details
    ISSN: 1432-2048
    Keywords: Auxin binding ; Auxin-binding protein ; Zea (auxin binding)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several properties of a 43-kilodalton (kDa) auxin-binding protein (ABP) having 22-kDa subunits are shared by a class of auxin binding designated Site I. The spatial distribution of the ABP in the maize (Zea mays L.) mesocotyl corresponds with the distribution of growth induced by naphthalene-1-acetic acid and with the distribution of Site I binding as previously shown by J.D. Walton and P.M. Ray (1981, Plant Physiol. 68, 1334–1338). The greatest abundance of both ABP and Site I activity is at the apical region of the mesocotyl. The ABP and Site I activity co-migrate in isopycnic centrifugation with the endoplasmic-reticulum marker, cytochrome-c reductase. Red light, at low and high fluence, far-red and white light were used to alter the elongation rate of apical 1-cm sections of etiolated maize mesocotyls, the amount of auxin binding, and the abundance of the ABP. Relative changes in auxin binding and the ABP were correlated, but the growth rate was not always correlated with the abundance of the ABP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391088
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  • 7
    Electronic Resource
    Electronic Resource
    Red-light-regulated growth (1998)
    Springer
    Planta 204 (1998), S. 207-211 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Auxin ; Growth ; Epidermis ; Indole-3-acetic acid ; Red light ; Zea (mesocotyl)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The etiolated maize (Zea mays L.) shoot has served as a model system to study red light (R)-regulated growth. Previous studies have shown that R inhibition of maize mesocotyl elongation involves a change in the auxin economy. Shown here is that R causes an increased tension in the epidermis relative to the inner tissue indicating that the growth of the epidermis is preferentially inhibited by R irradiation. This observation, taken together with previous indirect estimates of auxin within the epidermis, has prompted the hypothesis that R mediates the inhibition of mesocotyl elongation by preferentially decreasing auxin in the epidermis, a tissue which constrains the growth of the organ. We tested this hypothesis using gas chromatography-selected ion monitoring-mass spectrometry analysis of free indole-3-acetic acid (IAA) levels in both the apical 1 cm of the mesocotyl and the corresponding epidermis of etiolated and 4-h, R-irradiated seedlings. Red light irradiation caused a 1.4-fold reduction in free IAA within the whole section of the apical mesocotyl. However, within the peeled mesocotyl epidermis, R irradiation caused at least a 1.9-fold reduction in free IAA. To determine if the nearly twofold decrease in epidermal auxin occurring after R is physiologically significant, IAA was differentially applied to opposite sides of shoots. A twofold difference in IAA application rate caused asymmetrical growth. Thus, the twofold R-induced decrease in free IAA level in the epidermis, a difference sufficient to affect growth, and the rapid R-induced change in growth rate in the epidermis are consistent with the hypothesis that R causes growth of the mesocotyl to decrease by preferentially regulating the free IAA level in the mesocotyl epidermis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050248
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  • 8
    Electronic Resource
    Electronic Resource
    In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli (1993)
    Springer
    Plant molecular biology 21 (1993), S. 1191-1194 
    Details
    ISSN: 1573-5028
    Keywords: phytochrome ; chaperonins ; protein expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When expressed in Escherichia coli, a truncated form of phytochrome (oat PHYA AP3 residues 464-1129) self associates to form a series of products ranging in size from monomers to aggregates of greater than 20 subunits. When these same phytochrome sequences are coexpressed with the chaperonins GroEL and GroES, the truncated phytochrome migrates as a native-like dimer in size exclusion chromatography and no higher-order aggregates were detected. GroEL and GroES inhibition of phytochrome aggregation in E. coli presumably occurs via the suppression of folding pathways leading to incorrectly folded phytochrome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00023616
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  • 9
    Electronic Resource
    Electronic Resource
    Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions (1989)
    Springer
    Planta 178 (1989), S. 147-156 
    Details
    ISSN: 1432-2048
    Keywords: Avena (phytochrome) ; Phytochrome (structure, photoreversibility)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have undertaken a study of the structure of the amino-terminal domain of the phytochrome polypeptide purified from Avena sativa L. Amino-acid sequencing was used to indentify arginine 52 as the precise location of a conformation-specific cleavage of phytochrome by subtilisin. The location of the epitopes for a class of monoclonal antibodies designated type 2 has been shown to be located between approx. 10 and 20 kilodaltons (kDa) from the amino terminus. These two new spatial markers, in addition to the chromophore and another epitope recognized by type 1 monoclonal antibodies and located within 6 kDa from the amino terminus, have been used to map the locations of several new protease-accessible sites along the polypeptide. After extensive digestion of phytochrome with subtilisin, a stable spectrally-active group of peptides remains. Within this group is a 16-kDa chromopeptide which, either alone or as part of an assemblage of peptides, elutes from a size-exclusion column under nondenaturing conditions at a volume consistent with a molecular mass of 35–40 kDa. This group of peptides has an absorbance spectrum similar to the red-absorbing form of phytochrome (Pr) and is red/far-red photoreversible between this and a photobleached form. These data indicate that this group of peptides still retains the principal structural requisites for Pr-chromophore-protein interactions and for photoreversibility, but not for Pfr (far-red-absorbing phytochrome)-chromophore-protein interactions. It is uncertain if these structural requisites reside exclusively on the 16-kDa chromopeptide or result from an assemblage of these peptides. However, we have excluded any role for an adjacent 14-kDa fragment (approximately residues 50 to 200) in the observed spectral properties since it can be selectively removed without any effect on the photoreversibility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00393189
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  • 10
    Electronic Resource
    Electronic Resource
    Comparative compositional analysis of walls with two different morphologies: archetypical versus transfer-cell-like (1999)
    Springer
    Protoplasma 209 (1999), S. 238-245 
    Details
    ISSN: 1615-6102
    Keywords: Cell wall composition ; Maize endosperm ; Solute transport ; Transfer cells ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Abnormally thick cell walls of a clonal maize cell line with the labyrinth wall morphology found in transfer cells were analyzed and compared to the relatively thin and even archetypical walls of a sister cell line. Despite a drastic difference in wall morphology between the transfer and archetypical cell walls, the chemical composition of the walls was essentially the same. There were no major differences in the glycosyl residue composition, in the amount of total lipid, and in the amount of total protein. The amounts of wall material released by chemical extraction of cellulosic, hemicellulosic, and pectic fractions were the same for the two types of walls. There were some differences in the protein profile and in the inorganic ion content between the transfer and archetypical walls. These results indicate that profound changes in wall morphology can be brought about in the absence of gross changes in wall composition and suggest that major changes in time- or place-dependent deposition and/or subtle changes in arrangement of rare wall constituents may be responsible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01453452
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