A p34cdc2-based cell cycle: its significance in monocotyledonous, dicotyledonous and unicellular plants

John, Peter; Zhang, Kerong; Dong, Chongmei

doi:10.1007/978-94-011-1789-0_2

Cited by 21 publications

(17 citation statements)

References 58 publications

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“…There may have been a contribution from Cdc2 variants, but the measured activity in the p13 suc1 affinitypurified fraction was predominantly the mitotically active form of Cdc2, since activity of this enzyme is 4 times higher at mitosis than at other times in the cell cycle of plants (John et al, 1993;Zhang et al, 1996) and other organisms (for review, see Nurse, 1990;Stern and Nurse, 1996). We cannot eliminate the possibility of a minor contribution from variants of Cdc2, but activity from such variants has not yet been demonstrated unequivocally in plants.…”

Section: Speed Of Response Of Cdc2-like Kinase Activitymentioning

confidence: 92%

Effect of Water Stress on Cell Division and Cdc2-Like Cell Cycle Kinase Activity in Wheat Leaves1

et al. 1998

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In wheat (Triticum aestivum) seedlings subjected to a mild water stress (water potential of ؊0.3 MPa), the leaf-elongation rate was reduced by one-half and the mitotic activity of mesophyll cells was reduced to 42% of well-watered controls within 1 d. There was also a reduction in the length of the zone of mesophyll cell division to within 4 mm from the base compared with 8 mm in control leaves. However, the period of division continued longer in the stressed than in the control leaves, and the final cell number in the stressed leaves reached 85% of controls. Cyclindependent protein kinase enzymes that are required in vivo for DNA replication and mitosis were recovered from the meristematic zone of leaves by affinity for p13 suc1 . Water stress caused a reduction in H1 histone kinase activity to one-half of the control level, although amounts of the enzyme were unaffected. Reduced activity was correlated with an increased proportion of the 34-kD Cdc2-like kinase (an enzyme sharing with the Cdc2 protein of other eukaryotes the same size, antigenic sites, affinity for p13 suc1 , and H1 histone kinase catalytic activity) deactivated by tyrosine phosphorylation. Deactivation to 50% occurred within 3 h of stress imposition in cells at the base of the meristematic zone and was therefore too fast to be explained by a reduction in the rate at which cells reached mitosis because of slowing of growth; rather, stress must have acted more immediately on the enzyme. The operation of controls slowing the exit from the G1 and G2 phases is discussed. We suggest that a water-stress signal acts on Cdc2 kinase by increasing phosphorylation of tyrosine, causing a shift to the inhibited form and slowing cell production.A decrease in soil water potential due to drought or salinity decreases the rate of leaf expansion, whereas root expansion is much less affected (Munns and Sharp, 1993). If the root water potential decreases suddenly, the response of leaf expansion is so rapid and large (Cramer and Bowman, 1991) that it must be due to a change in the rate of expansion of existing cells, rather than to a change in the rate of production of new cells. However, when plants have grown for some time in soils of low water potential, smaller leaves with fewer cells are formed (Clough and Milthorpe, 1975;Randall and Sinclair, 1988;Lecoeur et al., 1995). These observations suggest that reduced cell formation during water stress may limit final leaf size.Little is known about the effects of water stress on rates of cell division or on mitotic activity in leaves. Roots have received more attention. In roots there was a rapid decrease in mitotic activity after imposition of water stress (Yee and Rost, 1982;Robertson et al., 1990b; Bitonti et al., 1991; Bracale et al., 1997), and a similar response was found for soybean hypocotyls (Edelman and Loy, 1987). These sudden decreases in mitotic activity suggest, but do not prove, that water stress caused a sudden decrease in the rate at which new cells were being produced. To our knowledge, the only ...

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Section: Speed Of Response Of Cdc2-like Kinase Activitymentioning

confidence: 92%

Effect of Water Stress on Cell Division and Cdc2-Like Cell Cycle Kinase Activity in Wheat Leaves1

et al. 1998

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“…Changes in hormones required for growth appear to act on these control points. Auxin level affects the duration of G 1 and G 2 (Bayliss 1985, John et al 1993a, 1993b. For example, the switch in a dividing cell culture to meristemlike growth after induction of embryogenesis by auxin withdrawal accelerated the cell cycle by shortening G 1.…”

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confidence: 99%

Immunocytochemical study of cell cycle control by cytokinin in cultured soybean cells

Mader

Hanke

1996

J Plant Growth Regul

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An immunocytochemical method was used to determine the proportion of cells in the DNA synthesis (S phase) of the mitotic cycle in suspension cultures of soybean (Glycine max (L.) Merr. cv. Acme) callus of cotyledonary origin, the stably cytokinin-dependent tissue used in the cytokinin bioassay devised by Carlos O.Miller. A standard cell synchronization protocol involving hydroxyurea was used to demonstrate the applicability of the immunocytochemical method to this cell culture. Cells were brought to mitotic arrest by cytokinin withdrawal, and the cell division cycle was restarted by the addition of cytokinin. We have followed the pattern of resumption of S phase after the readdition of cytokinin. This pattern reveals the existence of three subpopulations of cells in cytokinin-starved cultures, consistent with the occurrence of three cytokinin-requiring events in the cell cycle: one in mitosis, one in S phase, and one in the G~ phase.

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“…The protein, pl3sucl, is essential for the normal function of p34cdc2 kinase, which occupies a pivotal position in the control of cell division in eukaryotic organisms (1)(2)(3)(4), including plants (5). Depletion of the suci gene has shown that pl3sucl is necessary for the inactivation ofp34cdc2 at anaphase and for completion of mitosis.…”

mentioning

confidence: 99%

Nuclear concentration and mitotic dispersion of the essential cell cycle protein, p13suc1, examined in living cells.

Hepler

Sek

John

1994

Proc. Natl. Acad. Sci. U.S.A.

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Stamen hair cells of Trdescantia vwrginana have been microiqjected with pl311 labeled with carboxyfluorescein (CF) and studied trougout the division cycle in living cells by using the confocal laser snning microscope. The protein, pl3w"l, is essential for the rapid inactivation ofthe key mitotic catalyst, p34alc2 kinase, at anaphase and for completion of nuclear division. Duig interphase or prophase, CF-pl3Y' concentrates quickly (<2 min) in nuclei, reaching levels that are 2-fold greater than those in the cytoplasm. (7) and is indicated in vivo by the restoration of division in cells containing some mutant forms of p34cdc2, when pl3sucl is expressed at higher levels (8,9 MATERIALS AND METHODSPreparation of p13""' and Carboxyfluorescein (CF) Taggng. pl3sucl was obtained by overexpression in Escherichia coli, by using the strategy of Brizuela et al. (7), and was purified to homogeneity by chromatography on Sephadex G-75 and 2-phenyl-Sepharose, as described by John et al. (11). It was tagged as described for tubulin (15), by reaction for 1 hr at 250C with 5(6)-carboxyfluorescein-N-hydroxysuccinimide ester (Boehringer) at a dye-to-pl3sucl molar ratio of 40:1 in 54 mM NaHCO3, pH 8.5/46% (vol/vol) dimethyl sulfoxide, freed of unbound dye by Sephadex G-25 (Pharmacia) chromatography in 0.1 M NaHCO3 (pH 8.5) and a 10 x 300 mm column, and then dialyzed extensively against water at 40C. As shown in Fig. LA

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A p34cdc2-based cell cycle: its significance in monocotyledonous, dicotyledonous and unicellular plants

Cited by 21 publications

References 58 publications

Effect of Water Stress on Cell Division and Cdc2-Like Cell Cycle Kinase Activity in Wheat Leaves1

Effect of Water Stress on Cell Division and Cdc2-Like Cell Cycle Kinase Activity in Wheat Leaves1

Immunocytochemical study of cell cycle control by cytokinin in cultured soybean cells

Nuclear concentration and mitotic dispersion of the essential cell cycle protein, p13suc1, examined in living cells.

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