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Plant Physiol. (1998) 116: 1539-1549 Genes Involved in Osmoregulation during Turgor-Driven Cell Expansion of Developing Cotton Fibers Are Differentially Regulated1
Department of Vegetable Crops (L.B.S.), and Department of Agronomy and Range Science (F.V., T.A.W.), University of California, Davis, California 95616; and University of California, Davis, California 95616Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan (M.M.)
Cotton
(Gossypium hirsutum L.) fibers are single-celled
trichomes that synchronously undergo a phase of rapid cell
expansion, then a phase including secondary cell wall deposition, and
finally maturation. To determine if there is coordinated regulation of gene expression during fiber expansion, we analyzed the expression of
components involved in turgor regulation and a cytoskeletal protein by
measuring levels of mRNA and protein accumulation and enzyme activity.
Fragments of the genes for the plasma membrane proton-translocating
ATPase, vacuole-ATPase, proton-translocating pyrophosphatase (PPase),
phosphoenolpyruvate carboxylase, major intrinsic
protein, and
Plant cell expansion occurs through the interaction of multiple
influences, including cell wall-yield properties; the opposing force of
turgor pressure; the biosynthesis of new membrane lipids, cell wall
components, and proteins; and proper trafficking of these newly
synthesized materials to their final cellular destination. During
cell expansion the force of turgor pressure is related to the osmotic
potential and to the transport coefficient for water uptake (Cosgrove,
1986 The fiber cells of cotton (Gossypium hirsutum L.) represent
a single cell type that undergoes a period of very rapid elongation. Cotton fibers also represent an agricultural commodity of major economic importance in the United States. Fiber cells are single-celled trichomes, which arise in near synchrony from the epidermis of the
ovule and may elongate at peak rates in excess of 2 mm
d In this work we have assayed the expression of several components,
outlined below, involved in cell expansion at the levels of RNA
accumulation, protein accumulation, and enzymatic activity throughout
fiber development. The V-ATPase and PPase, as mentioned above, are
responsible for driving solute movement into the vacuole, which is
important for maintaining the osmotic potential necessary to generate
turgor pressure. The PM H+-ATPase translocates
protons out of the cytosol, acidifying the apoplast, which is theorized
to effect a change in cell wall extensibility (Rayle and Cleland,
1992 Growth Conditions
Isolation of Cotton DNA and RNA Genomic DNA was isolated from young, expanding leaves of cotton as described (Wilkins et al., 1994 ). For RNA, developing fibers were
collected from bolls by freezing the excised ovules in liquid N2, and then brushing off the protruding fiber cells. The
isolated fiber cells from +5, +10, +15, +20, +25, and +30 dpa were used for RNA extraction (Wan and Wilkins, 1994b; Wilkins and Smart, 1996).
Purified total RNA was divided into aliquots, precipitated with
ethanol, and stored at  80°C under 70% (v/v) ethanol. For RPAs, the
RNA pellets were collected by centrifugation and the pellet was dried
under vacuum, and then resuspended to a final concentration of 0.2 mg
mL 1 in diethyl pyrocarbonate-treated water.
PCR Amplification and Cloning PCR was used to amplify partial cDNAs encoding the PM H+-ATPase, PEPCase, MIP, and -tubulin from
approximately 1 × 109 plaque-forming units
of a cotton +10-dpa fiber cDNA library constructed in the phagemid
vector  ZAPII (Stratagene). First-strand cDNA from
reverse-transcribed RNA isolated from +10-dpa cotton ovule and fiber
tissue was used as the template for PCR amplification of the PPase.
Oligonucleotide PCR primer sequences, expected product size, and source
targets are listed in Table I. PCR
mixture was 1× PCR buffer (10 mm Tris-HCl [pH 8.3] and
50 mm KCl), 1.5 mm MgCl2,
0.8 mm dNTPs, 1.0 µm of each oligonucleotide
primer, and 2.5 units of Taq DNA polymerase. Reactions (50 µL) were performed in either a Perkin-Elmer model 480 or an Ericomp
thermal cycler (San Diego, CA) using the annealing temperatures listed
in Table I. A portion of the cDNA CVA69.24 (Wilkins, 1993), which
encodes the 69-kD subunit of the V-ATPase from cotton, was PCR
amplified from plasmid DNA containing the cloned cDNA using the above
conditions. A portion of the 18S rRNA gene was amplified from cotton
genomic DNA using the above conditions. Amplification products from all of the reactions described above were subcloned into the plasmid vector
pCRII (Invitrogen, San Diego, CA). Cloned products encoding PEPCase and
18S rRNA were further subcloned into the plasmid vector pBluescript II
(Stratagene) to facilitate synthesis of in vitro-transcribed probes for
RPAs. The DNA sequences of the cloned fragments to be used as probes
were determined from both strands using the Sequenase version II
dideoxy sequencing kit according to the manufacturer (Amersham) or
using an automated sequencing system (Applied Biosystems). Sequence
analysis was performed using either MacDNASIS (Hitachi Software, Palo
Alto, CA) or PCGene (IntelliGenetics, Campbell, CA).
RPAs RPAs were performed using the HybSpeed RPA kit essentially as described by the manufacturer (Ambion, Austin, TX). RNA probes were synthesized by in vitro transcription from linearized plasmid DNA in the presence of 50 µCi of-[32P]UTP (3000 Ci mmol1) (Dupont/NEN) using either
T7 or SP6 RNA polymerase and were labeled to a
specific activity of approximately 1 × 109
cpm µg1. The 18S rRNA probe was synthesized
using 1 µCi of -[32P]UTP together with the
T7 Megashortscript kit as described by the
manufacturer (Ambion) and was labeled to a specific activity of
approximately 5 × 104 cpm
µg1. Full-length transcripts for probes were
purified after electrophoresis in a 5% (w/v) denaturing polyacrylamide
vertical slab gel. Trial reactions using 0.2, 1.0, and 2.5 µg of RNA
were performed, and a linear increase was observed when comparing the
signal from the 1.0-µg sample to that of the 2.5-µg sample,
indicating that the reactions were not saturated, even for the 18S rRNA
probe (data not shown). One microgram of total cotton fiber RNA was hybridized with 2 × 104 cpm of radiolabeled
probe for each reaction, except for the 18S rRNA probe, in which 3 × 103 cpm were added. RPA reaction products were
resolved by electrophoresis in a 5% denaturing polyacrylamide gel
poured using an analytical comb and electrophoresed using an S2 gel
electrophoresis apparatus for optimum resolution (Gibco-BRL). These
gels were treated with a solution of 10% (v/v) ethanol, 10% (v/v)
acetic acid, transferred to chromatography paper, and then vacuum
dried. Protected products were detected by autoradiography at 80°C
using reflection film and intensifying screens (DuPont/ NEN), and a
radioactive signal was quantified by phosphor imagery (Fujix BAS1000,
Fuji Film Co., Tokyo, Japan). If the RPA yielded a doublet of bands,
then the combined intensity of both bands was quantified. The sizes of protected products were compared with the migration of radiolabeled products generated from the Century RNA Size Marker kit (Ambion). Assays were repeated at least three times.
Preparation of Microsomal Membranes and Tonoplast Microsomal membranes were prepared essentially as described (Bennett et al., 1984) with some modification to enhance the microsomal preparation, particularly at +10 and +15 dpa. Cotton ovules were isolated and blended in homogenization medium (0.35 mm Suc,
70 mm Tris-HCl [pH 8.0], 10% [v/v] glycerol, 3 mm Na2EDTA, 0.15% [w/v] BSA, 1.5%
[w/v] PVP-40, 4 mm DTT, and 1.5 mm PMSF) with a chilled Waring blender for a few seconds. Ovules of +15 dpa and older
stages were cut with scissors into small pieces before homogenization.
The tissue homogenate was set aside at 0°C for 10 to 15 min to allow
foam to settle and was then filtered through three layers of Miracloth
(Calbiochem). The filtrate was centrifuged for 15 min at
15,000g at 4°C, and the resulting pellet was discarded. A
2-mL portion of the supernatant was saved as the enzyme extract for
PEPCase activity determination. The remainder of the filtrate was
centrifuged at 100,000g at 4°C for 40 min, and the
microsomal pellet was resuspended in RM (0.35 m Suc, 10 mm Tris-Mes [pH 7.0], 2 mm DTT, and 1.5 mm PMSF). The microsomal suspensions were frozen in liquid
nitrogen and saved at 80°C until the next day for enzyme assays or
for further membrane purification. Resuspended microsomal membranes
were centrifuged in an Eppendorf centrifuge at 16,000g at
4°C for 5 min, and the resulting supernatant was used as the soluble
protein fraction for enzyme assays.
Purification of Cotton Ovule PM The PM of cotton ovules were purified by two-phase partitioning (Kjellbom and Larsson, 1984; Larsson, 1985). The microsomal pellet, as
prepared above, was resuspended in 0.33 m Suc, 5 mm KCl, and 5 mm potassium phosphate (pH 7.8).
One gram of the suspension containing about 6 mg of protein was added
to the 7-g phase mixture to give an 8-g phase system with a final
composition of 6.5% (w/w) PEG (Mr = 3350),
6.5% (w/w) dextran T-500, 0.33 m Suc, 5 mm
KCl, and 5 mm potassium phosphate (pH 7.8). The phase
system was thoroughly mixed by 20 to 30 inversions of the tube, then
phase separation was facilitated by centrifugation in a swinging bucket
rotor at 2000g, at 4°C for 5 min. The PM partitioned into
the PEG-rich upper phase, whereas the intracellular membranes
partitioned at the interface and in the dextran-rich lower phase
(Larsson and Anderson, 1979). The upper phase was removed and
repartitioned two additional times with fresh lower phase. The final
upper phases were diluted at least 2-fold with RM, and the PM was
collected by ultracentrifugation at 100,000g at 4°C for 20 min. The pellet was washed twice with RM, and the pure PM pellet was
resuspended in RM for use in enzyme assays.
Protein Assays Protein concentration was measured by the dye-binding method (Bradford, 1976) using BSA as a protein standard. Membrane protein in
RM was first solubilized in 0.05% (v/v) Triton X-100 before the
addition of the dye reagent (Bio-Rad). The final concentration of
Triton X-100 in the protein assay mixture was 0.005% (v/v).
Enzyme Assays ATPase activity was assayed as the liberation of Pi from either ATP or PPi and was detected colorimetrically (Ames, 1966; Bennett et
al., 1988). ATP and PPi were purchased as disodium salts (Sigma). To
deplete the ATP and PPi of sodium ions, they were first treated with
HCl, and then desalted with Dowex 50W resin. Finally, the pH was
adjusted to 6.5 with BTP (bis-Tris propane
[1,3-bis(Tris-[hydroxymethyl]methylamino) propane]). The reaction
was initiated by the addition of 8 to 12 µg of membrane protein to a
0.4-mL reaction volume, and the reaction was incubated at 30°C for 30 min. The reactions were terminated and measured spectrophotometrically
at 820 nm, as described (Ames, 1966).
Denaturing Gel Electrophoresis and Immunoblotting SDS-PAGE was performed using 10% (w/v) polyacrylamide gels with Laemmli buffers (Laemmli, 1970) and the Mini Protean II electrophoresis system (Bio-Rad). Antibodies raised against V-ATPase, PM
H+-ATPase, PPase, PEPCase, MIP, or -tubulin
(Table II) were used for estimating the
relative abundance of each protein during development of the cotton
ovules. Protein resolved by SDS-PAGE was immediately transferred to
PVDF membrane (Millipore) in a Trans-Blot Cell (Bio-Rad) (Towbin et
al., 1979). The blots were blocked with 1% (w/v) nonfat dry milk and
0.4% (v/v) Tween 20 in PBS for 2 h at 23°C, and probed with the
appropriate antisera (Table II) for 16 h at 23°C. Nonbinding
primary antibody was removed by rinsing with PBS. Positive antibody
reaction was detected with protein A-alkaline phosphatase conjugate
reacted with 5-bromo-4-chloro-3 indolyl phosphate and nitroblue
tetrazolium. Relative intensities of the colorimetric reaction products
on the immunoblots blots were determined by densitometric scanning
using an imaging densitometer (model GS-670, Bio-Rad).
PCR Amplification and Cloning To obtain probes to assay transcript accumulation throughout development of fiber cells, PCR was used to amplify portions of genes encoding the PM H+-ATPase, the 69-kD subunit of the V-ATPase, PPase, PEPCase,-tubulin, and MIP from developing
cotton fibers. All of the amplified products were ligated into the
plasmid vector pCRII (Invitrogen) and transformants were screened for
the presence of the expected size insert (Table I). A portion of those
plasmids with the expected size insert were used to obtain partial
nucleotide sequence to verify the identity of those clones. Individual
clones chosen to be used as probes were sequenced completely, and the
sequences not previously reported, excluding the primer sequences, were
deposited in GenBank and given the following accession numbers:
PEPCase, AF008940; -tubulin, AF009565; PM
H+-ATPase, AF009566; MIP, AF009567; and PPase,
AF009568. Determination that a clone encodes a particular protein was
based on sequence comparison with published gene sequences.
Assays of Transcript Accumulation RPAs were utilized to measure the relative transcript abundance of the aforementioned genes during the expansion of developing cotton fibers (Fig. 1). Accumulation of transcripts encoding the PM H+-ATPase was highest during the phase of rapid elongation, from +5 dpa through +15 dpa. In fibers +20 dpa and older, PM H+-ATPase gene transcript abundance dropped to one-fourth of the level of that in fibers earlier in development. A similar pattern was observed for transcripts encoding the 69-kD subunit of the V-ATPase, confirming results of another study (T.A. Wilkins, C.-Y. Wan, W. Kim, F. Vojdani, and M.-P. Hasenfratz, unpublished data). Message levels for-tubulin
followed a similar pattern as for the ATPases, with peak accumulation
at +10 and +15 dpa, although the rise and decline of message levels
appeared to occur at a slower rate. This peak period of mRNA
accumulation corresponds to the period of most rapid cell expansion
(Basra and Malik, 1984; T.A. Wilkins, C.-Y. Wan, W. Kim, F. Vojdani,
and M.-P. Hasenfratz, unpublished data). The accumulation of mRNA
encoding PEPCase and MIP was highest in the earlier stages (+5 and +10
dpa), but then declined after +15 dpa. The detection of MIP mRNA
accumulation required much longer exposures, even though all of the
mRNA probes were labeled to approximately the same specific activity.
Exposure in the +30 dpa lane in Figure 1A was not due to hybridization of the MIP probe, but rather was a signal from a radiolabeled size
ladder in the adjacent lane (not shown). In contrast to the two
ATPases, the accumulation of transcript encoding the PPase was
constitutive through all stages of fiber development.
Immunoblot Analysis of Protein Accumulation To assay protein accumulation throughout development, immunoblotting was performed using protein isolated from developing ovules and fibers harvested starting at3 dpa through +35 dpa (Figs.
2 and 3).
Initially, protein was also extracted from only fibers at the later
developmental stages and used for comparison with protein from ovules
and fibers. Immunoblots probed for V-ATPase protein indicated
comparable patterns of accumulation throughout development, except for
a slightly higher level of V-ATPase protein in the ovule plus fiber
extract compared with fiber protein between +15 and +20 dpa (data not
shown), which is the period when the embryo enlarges (Wilkins and
Jernstedt, 1997).
Enzyme Activity Assays The ATPase activity of the PM H+-ATPase and the V-ATPase were assayed in microsomes (data not shown) and in PM- or tonoplast-enriched fractions (Fig. 4) using a published procedure that relies on the differential sensitivity of the V- and P-type ATPases to inhibitors (Gallagher and Leonard, 1982; Bennett et al., 1984). The pyrophosphatase activity of the PPase
was also measured in microsomes (data not shown) and tonoplast-enriched
fractions (Fig. 4) as described (Rea and Poole, 1985). Care was taken
to measure enzyme activity as soon as possible after protein
purification and to use samples that had experienced minimal
freeze/thaw cycles, since activity does decrease slightly over time and
after a freeze/thaw event (data not shown). The activity of the PM
H+-ATPase displays the lowest levels of activity
early and late in fiber development (<+10 dpa and >+25 dpa), whereas
the highest activity was measured in samples from +15 dpa. The activity
of the PM H+-ATPase was highly enriched in PM
purified by two-phase partitioning (Fig. 4) as compared with activity
in total microsomes (data not shown). The activity of the V-ATPase
displayed a very similar pattern through development, with peak
activity at +15 dpa. As with both H+-ATPases, the
PPase displayed rising levels of activity in samples from +3 through
+15 dpa but, in contrast, the peak of PPase activity was at +20 dpa
rather than +15 dpa. Likewise, the activities of the vacuolar enzymes
were greater in tonoplast-enriched fractions isolated by Suc
density-gradient fractionation (Fig. 4) than in total microsomes (data
not shown). The patterns of enzyme activity in total microsomes were
essentially equivalent to the patterns observed in enriched membrane
preparations, indicating that enrichment for the membrane fractions was
performed with equivalent efficiency throughout the developmental
series. The activity of PEPCase was measured in total protein (Fig. 4).
Highest PEPCase activity levels were measured in samples from 1 dpa,
which represents a sharp increase from the activity at 3 dpa.
Activity declined through +10 dpa, with another peak at +15 dpa, then
declined again through fiber development.
The regulation of cell expansion is a vital process of plant
growth and development and is subject to control by environmental and
hormonal factors. Cotton fibers afford us the opportunity to study the
development of a single cell type that undergoes very rapid, virtually
synchronized cell elongation (Basra and Malik, 1984
2 Present address: State University of New York (SUNY) College of Environmental Science and Forestry, Faculty of Environmental and Forest Biology, One Forestry Drive, 302 Illick Hall, Syracuse, NY 13210. 3 These authors contributed equally to the paper. * Corresponding author; e-mail tawilkins{at}ucdavis.edu; fax 1-916-752-4361. Received November 14, 1997;
accepted December 8, 1997.
Abbreviations:
dpa, days postanthesis.
H+-ATPase, proton-translocating ATPase.
LPC, l-
The authors are grateful to Dr. Alan B. Bennett for allowing
some of this work to be performed in his laboratory and to Dr. Ching-Yi
Wan for isolating the
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  X. Yang, L. Tu, L. Zhu, L. Fu, L. Min, and X. Zhang Expression profile analysis of genes involved in cell wall regeneration during protoplast culture in cotton by suppression subtractive hybridization and macroarray J. Exp. Bot., October 1, 2008; 59(13): 3661 - 3674. [Abstract] [Full Text] [PDF]
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 S. Lv, K. Zhang, Q. Gao, L. Lian, Y. Song, and J. Zhang Overexpression of an H+-PPase Gene from Thellungiella halophila in Cotton Enhances Salt Tolerance and Improves Growth and Photosynthetic Performance Plant Cell Physiol., August 1, 2008; 49(8): 1150 - 1164. [Abstract] [Full Text] [PDF]
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S. K. Delaney, S. J. Orford, M. Martin-Harris, and J. N. Timmis The Fiber Specificity of the Cotton FSltp4 Gene Promoter is Regulated by an AT-Rich Promoter Region and the AT-Hook Transcription Factor GhAT1 Plant Cell Physiol., October 1, 2007; 48(10): 1426 - 1437. [Abstract] [Full Text] [PDF]
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L. Li, X.-L. Wang, G.-Q. Huang, and X.-B. Li Molecular characterization of cotton GhTUA9 gene specifically expressed in fibre and involved in cell elongation J. Exp. Bot., September 1, 2007; 58(12): 3227 - 3238. [Abstract] [Full Text] [PDF]
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 Y.-H. Shi, S.-W. Zhu, X.-Z. Mao, J.-X. Feng, Y.-M. Qin, L. Zhang, J. Cheng, L.-P. Wei, Z.-Y. Wang, and Y.-X. Zhu Transcriptome Profiling, Molecular Biological, and Physiological Studies Reveal a Major Role for Ethylene in Cotton Fiber Cell Elongation PLANT CELL, March 1, 2006; 18(3): 651 - 664. [Abstract] [Full Text] [PDF]
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Y. Wu, A. C. Machado, R. G. White, D. J. Llewellyn, and E. S. Dennis Expression Profiling Identifies Genes Expressed Early During Lint Fibre Initiation in Cotton Plant Cell Physiol., January 1, 2006; 47(1): 107 - 127. [Abstract] [Full Text] [PDF]
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 K. D. Cameron, M. A. Teece, and L. B. Smart Increased Accumulation of Cuticular Wax and Expression of Lipid Transfer Protein in Response to Periodic Drying Events in Leaves of Tree Tobacco Plant Physiology, January 1, 2006; 140(1): 176 - 183. [Abstract] [Full Text] [PDF]
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Y. Sun, S. Veerabomma, H. A. Abdel-Mageed, M. Fokar, T. Asami, S. Yoshida, and R. D. Allen Brassinosteroid Regulates Fiber Development on Cultured Cotton Ovules Plant Cell Physiol., August 1, 2005; 46(8): 1384 - 1391. [Abstract] [Full Text] [PDF]
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X.-B. Li, X.-P. Fan, X.-L. Wang, L. Cai, and W.-C. Yang The Cotton ACTIN1 Gene Is Functionally Expressed in Fibers and Participates in Fiber Elongation PLANT CELL, March 1, 2005; 17(3): 859 - 875. [Abstract] [Full Text] [PDF]
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Y.-L. Ruan, S.-M. Xu, R. White, and R. T. Furbank Genotypic and Developmental Evidence for the Role of Plasmodesmatal Regulation in Cotton Fiber Elongation Mediated by Callose Turnover Plant Physiology, December 1, 2004; 136(4): 4104 - 4113. [Abstract] [Full Text] [PDF]
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S. Padmanaban, X. Lin, I. Perera, Y. Kawamura, and H. Sze Differential Expression of Vacuolar H+-ATPase Subunit c Genes in Tissues Active in Membrane Trafficking and Their Roles in Plant Growth as Revealed by RNAi Plant Physiology, April 1, 2004; 134(4): 1514 - 1526. [Abstract] [Full Text] [PDF]
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 G. J. WAGNER, E. WANG, and R. W. SHEPHERD New Approaches for Studying and Exploiting an Old Protuberance, the Plant Trichome Ann. Bot., January 1, 2004; 93(1): 3 - 11. [Abstract] [Full Text] [PDF]
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L.-H. Liu, U. Ludewig, B. Gassert, W. B. Frommer, and N. von Wiren Urea Transport by Nitrogen-Regulated Tonoplast Intrinsic Proteins in Arabidopsis Plant Physiology, November 1, 2003; 133(3): 1220 - 1228. [Abstract] [Full Text] [PDF]
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Y.-Q. Zhu, K.-X. Xu, B. Luo, J.-W. Wang, and X.-Y. Chen An ATP-Binding Cassette Transporter GhWBC1 from Elongating Cotton Fibers Plant Physiology, October 1, 2003; 133(2): 580 - 588. [Abstract] [Full Text] [PDF]
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 S.-J. Ji, Y.-C. Lu, J.-X. Feng, G. Wei, J. Li, Y.-H. Shi, Q. Fu, D. Liu, J.-C. Luo, and Y.-X. Zhu Isolation and analyses of genes preferentially expressed during early cotton fiber development by subtractive PCR and cDNA array Nucleic Acids Res., May 15, 2003; 31(10): 2534 - 2543. [Abstract] [Full Text] [PDF]
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X.-B. Li, L. Cai, N.-H. Cheng, and J.-W. Liu Molecular Characterization of the Cotton GhTUB1 Gene That Is Preferentially Expressed in Fiber Plant Physiology, October 1, 2002; 130(2): 666 - 674. [Abstract] [Full Text] [PDF]
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I. Hakman and P. Oliviusson High expression of putative aquaporin genes in cells with transporting and nutritive functions during seed development in Norway spruce (Picea abies) J. Exp. Bot., April 1, 2002; 53(369): 639 - 649. [Abstract] [Full Text] [PDF]
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X. Chen, T. Kanokporn, Q. Zeng, T. A. Wilkins, and A. J. Wood Characterization of the V-type H(+)-ATPase in the resurrection plant Tortula ruralis: accumulation and polysomal recruitment of the proteolipid c subunit in response to salt-stress J. Exp. Bot., February 1, 2002; 53(367): 225 - 232. [Abstract] [Full Text] [PDF]
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H. J. Kim and B. A. Triplett Cotton Fiber Growth in Planta and in Vitro. Models for Plant Cell Elongation and Cell Wall Biogenesis Plant Physiology, December 1, 2001; 127(4): 1361 - 1366. [Full Text] [PDF]
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V. T. Ciavatta, R. Morillon, G. S. Pullman, M. J. Chrispeels, and J. Cairney An Aquaglyceroporin Is Abundantly Expressed Early in the Development of the Suspensor and the Embryo Proper of Loblolly Pine Plant Physiology, December 1, 2001; 127(4): 1556 - 1567. [Abstract] [Full Text] [PDF]
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K.J. Dietz, N. Tavakoli, C. Kluge, T. Mimura, S.S. Sharma, G.C. Harris, A.N. Chardonnens, and D. Golldack Significance of the V-type ATPase for the adaptation to stressful growth conditions and its regulation on the molecular and biochemical level J. Exp. Bot., October 1, 2001; 52(363): 1969 - 1980. [Abstract] [Full Text] [PDF]
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Y.-L. Ruan, D. J. Llewellyn, and R. T. Furbank The Control of Single-Celled Cotton Fiber Elongation by Developmentally Reversible Gating of Plasmodesmata and Coordinated Expression of Sucrose and K+ Transporters and Expansin PLANT CELL, January 1, 2001; 13(1): 47 - 60. [Abstract] [Full Text]
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 K. Schumacher, D. Vafeados, M. McCarthy, H. Sze, T. Wilkins, and J. Chory The Arabidopsis det3 mutant reveals a central role for the vacuolar H+-ATPase in plant growth and development Genes & Dev., December 15, 1999; 13(24): 3259 - 3270. [Abstract] [Full Text]
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D. J. Whittaker and B. A. Triplett Gene-Specific Changes in alpha -Tubulin Transcript Accumulation in Developing Cotton Fibers Plant Physiology, September 1, 1999; 121(1): 181 - 188. [Abstract] [Full Text]
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 J. Van't Hof Increased nuclear DNA content in developing cotton fiber cells Am. J. Botany, June 1, 1999; 86(6): 776 - 779. [Abstract] [Full Text] [PDF]
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H. Sze, X. Li, and M. G. Palmgren Energization of Plant Cell Membranes by H+-Pumping ATPases: Regulation and Biosynthesis PLANT CELL, April 1, 1999; 11(4): 677 - 690. [Full Text]
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Y.-L. Ruan and P. S. Chourey A Fiberless Seed Mutation in Cotton Is Associated with Lack of Fiber Cell Initiation in Ovule Epidermis and Alterations in Sucrose Synthase Expression and Carbon Partitioning in Developing Seeds Plant Physiology, October 1, 1998; 118(2): 399 - 406. [Abstract] [Full Text]
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Top
Abstract
Introduction
-tonoplast intrinsic protein from A. thaliana (75% identity, accession no. 
) and the 57-kD subunit (
). In the PEPCase panel, quantifications of the 100-kD band
(
-glucanase are expressed at highest levels between +9 and
+15 dpa (Shimizu et al., 1997
-TIP creates water specific channels in Xenopus oocytes.
EMBO J
12:
2241-2247