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1

Electronic Resource

Phytochrome-mediated swelling of etiolated leaf protoplasts and its possible biological significance (1990)

Zhou, Shubo ; Jones, Alan M. ; Scott, Tom K.

Springer

Plant cell reports 9 (1990), S. 435-438

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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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2

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Comparison of Site I auxin binding and a 22-kilodalton auxin-binding protein in maize (1989)

Jones, Alan M. ; Lamerson, Patrick ; Venis, Michael A.

Springer

Planta 179 (1989), S. 409-413

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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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3

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Red-light-regulated growth (1998)

Barker-Bridgers, Michele ; Ribnicky, David M. ; Cohen, Jerry D. ; [et al.]

Springer

Planta 204 (1998), S. 207-211

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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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4

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In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli (1993)

Edgerton, Michael D. ; Santos, Michael O. ; Jones, Alan M.

Springer

Plant molecular biology 21 (1993), S. 1191-1194

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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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5

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Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions (1989)

Jones, Alan M. ; Quail, Peter H.

Springer

Planta 178 (1989), S. 147-156

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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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6

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Comparative compositional analysis of walls with two different morphologies: archetypical versus transfer-cell-like (1999)

DeWitt, Greg ; Richards, Jason ; Mohnen, Debra ; [et al.]

Springer

Protoplasma 209 (1999), S. 238-245

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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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7

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Organ distribution of auxin-binding protein 1 in the etiolated maize seedling (1995)

Harnden, Daniel ; Jones, Alan M.

Springer

Journal of plant growth regulation 14 (1995), S. 109-113

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ISSN: 1435-8107

Source: Springer Online Journal Archives 1860-2000

Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition

Notes: Abstract The auxin-binding protein designated ABP1 has been proposed to mediate auxin-induced cellular changes such as cell expansion. Its exact mode of action is unknown, but currently several approaches to elucidate its function are being pursued. One of these approaches, described here, is to determine the organ distribution of this putative auxin receptor in order to correlate spatially the abundance of the protein with some auxin-regulated activity such as cell elongation. The absolute and relative amounts of ABP1 were determined along the entire etiolated shoot, the root, and within the caryopsis of maize. ABP1 can be detected immunologically in all extracts of the etiolated maize seedling except the tip of the primary root and the endosperm. Within the shoot, but excluding the leaf roll, the highest levels compared on a fresh weight basis are in the apical mesocotyl and basal coleoptile regions, the areas of the most rapid cell elongation and the areas where there is the greatest capacity for auxin-induced growth. The relative abundance of ABP1 compared on a fresh weight basis changed more than fivefold in this organ. When compared on a total protein basis, the relative change in ABP1 abundance was approximately two-fold, which is less than the relative change in auxin-induced growth rate along the shoot. Differences in shoot growth rate among varieties of maize were compared with the relative amounts of ABP1 within the apical mesocotyl and basal coleoptile. A statistically significant but not perfect correlation was found between the auxin-induced growth rate of the apical mesocotyl and ABP1 abundance. These results demonstrate a general correlation between the amount of ABP1 and growth along the shoot and within maize hybrid varieties.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00203122

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