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160 T. Müller, W. Koch, D. Wipf et al. 1993), and are characterized by a high affinity for cationic AA. The plant membranes maintain a proton gradient over the plasma membrane via plasma membrane ATPases, and, correspondingly, the first plant memberoftheAPCfamily,AtCAT1, mediated the accumulation of histidine in a pH-dependent manner (Frommer et al. 1995). However, it remains unclear whether AtCAT1 functions as a uniporter or an exchanger, or as a secondary active proton cotransporter. Recent studies of a related protein, AtCAT5, showed that the transport of basic AA mediated by AtCAT5 is sensitive to protonophores, indicating that at least AtCAT5 is a proton symporter. AtCAT5 is a high-affinity transporter for arginin with an apparent Km value of 12 µM (Su et al. 2004). Other basic AA were good competitors for 14 C arginine uptake into yeast cells expressing AtCAT5, while neutral or acidic AA like aspartate, proline, glutamate and glutamine were less effective in uptake inhibition. The transport selectivity of AtCAT5 is similar to that of AtCAT1, which also transports basic AA preferentially. For other members of the CAT-family in Arabidopsis no direct transport activity was demonstrated, nevertheless AtCAT3 and AtCAT6 expressed in yeast cells increased toxicity to the toxic analogue of glutamine, (S)-2 amino-6-diazo-5-oxo-L-norleucine, but not to the arginine analog canavanine (Su et al. 2004). The fact that arginine is not a substrate for AtCAT3 and AtCAT6 already shows that not all members of the CAT family in Arabidopsis canbesupposedtobecationicAAtransporters. In animals, the APC-type AA transporters require an additional subunit for functional expression at the plasma membrane (Sect. 11.2.3). Members of the mammalian CAT family essentially transport cationic AA by facilitateddiffusion,whiletheHATsareincontrastquitediverseintermsof substrate selectivity and function as obligatory exchangers. In plants no homologs of secondary subunits have yet been identified, and one subbranch of the APC family, the LAT (Fig. 11.2), have still not been functionally characterized in plants. 11.3.2 Amino Acid Transporter Family 1 Members of the ATF1 family were first described in plants as functional AA transporters. Structurally related proteins were identified in yeasts and animals (Fischer et al. 1998). The superfamily contains plant-specific subbranches, and branches that are more structurally related to mammalian transporters (Fig. 11.3). Within the plant-specific subbranches, the best-characterized members are the Arabidopsis AA permeases (AAP; Figs. 11.3, 11.4). Several AAP have been isolated from Arabidopsis by complementation of yeast transport mutants with plant cDNAs (Fischer et al.
11 AA transport in plant versus neutrotransmission 161 Fig.11.2. Phylogenetic tree of the AA–polyamine–choline (APC) superfamily (SLC7) (Hs Homo sapiens, At Arabidopsis thaliana). Maximum parsimony analyses were performed using PAUP 4.0b10 (Swofford 1998). Heuristic tree searches were executed using 100 random sequence additions and the tree bisection–reconnection branch-swapping algorithm with random sequence analysis. The complete alignment was based on 691 sites; 586 were phylogenetically informative. Bootstrap values (%) are indicated at branch nodes 1995; Frommer et al. 1993; Hsu et al. 1993; Kwart et al. 1993; Rentsch et al. 1996). AAP mediate H + -coupled uptake of a wide spectrum of AA when expressed in oocytes (Fischer et al. 2002). AtAAP1-5 represent low-affinity transporters with low selectivity towards AA side chains; only AAP3 and AAP5 transport basic AA efficiently. AAP6 has an approximately tenfold higher affinity towards all substrates when compared with other AAP. For glutamine, glutamate and asparagine, major transport forms of organic
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František Baluška · Stefano Manc
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Dr. František Baluška University
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VI Preface turn, reward the ants by
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VIII Preface of olfactory response.
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Contents 1 The Green Plant as an In
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Contents XIII 6 Signals and Targets
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Contents XV 11 Amino Acid Transport
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Contents XVII 15 Regulation of Plan
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Contents XIX 21.3 Conclusions and P
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Contents XXI 27.3.2 Catechin Induce
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XXIV Contributors Correa-Aragunde,
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XXVI Contributors Lamattina, L. (e-
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XXVIII Contributors Song, C. Depart
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1 The Green Plant as an Intelligent
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2 Neurobiological View of Plants an
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38 P.W. Barlow Thestimulipresentedt
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40 P.W. Barlow that a tropism is su
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42 P.W. Barlow the auxin flow into
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44 P.W. Barlow afferentnervousimpul
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46 P.W. Barlow analysis. In particu
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48 P.W. Barlow reception of his boo
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50 P.W. Barlow Iijima M, Kono Y (19
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4 How Can Plants Choose the Most Pr
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66 P.M. Neumann Finally, I examined
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68 P.M. Neumann evolutionary progre
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70 P.M. Neumann conclusion is that
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72 P.M. Neumann resources from matu
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6 Signals and Targets Triggered by
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6TargetsofSI 77 6.1.2 Self-Incompat
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6TargetsofSI 79 by Yang 2002) has p
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6TargetsofSI 81 al. 2002). Thus, SI
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6TargetsofSI 83 Fig.6.2. PrABP80 ha
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6TargetsofSI 85 many of the genes e
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6TargetsofSI 87 [Ca 2+ ]i may signa
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6TargetsofSI 89 is crosstalk betwee
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6TargetsofSI 91 Hepler PK, Vidali L
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6TargetsofSI 93 Snowman BN, Kovar D
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96 T. Nürnberger, B. Kemmerling Wh
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98 T. Nürnberger, B. Kemmerling Fo
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100 T. Nürnberger, B. Kemmerling p
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102 T. Nürnberger, B. Kemmerling i
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104 T. Nürnberger, B. Kemmerling r
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106 T. Nürnberger, B. Kemmerling F
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108 T. Nürnberger, B. Kemmerling M
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210 E.B. Blancaflor, K.D. Chapman v
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212 E.B. Blancaflor, K.D. Chapman l
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214 E.B. Blancaflor, K.D. Chapman N
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216 E.B. Blancaflor, K.D. Chapman 1
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218 E.B. Blancaflor, K.D. Chapman G
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15 Regulation of Plant Growth and D
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16 Physiological Roles of Nonselect
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16 Nonselective cation channels 237
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Fig.16.1. Possible roles of nonsele
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17 Touch-Responsive Behaviors and G
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18 Oscillations in Plants Sergey Sh
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18 Oscillations in Plants 263 Tempo
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18 Oscillations in Plants 265 Dries
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18 Oscillations in Plants 267 backg
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18 Oscillations in Plants 269 The f
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18 Oscillations in Plants 271 prehe
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18 Oscillations in Plants 273 Cardo
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18 Oscillations in Plants 275 Shaba
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278 K.Trebacz,H.Dziubinska,E.Krol W
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280 K.Trebacz,H.Dziubinska,E.Krol T
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282 K.Trebacz,H.Dziubinska,E.Krol E
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284 K.Trebacz,H.Dziubinska,E.Krol 1
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286 K.Trebacz,H.Dziubinska,E.Krol n
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288 K.Trebacz,H.Dziubinska,E.Krol D
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290 K.Trebacz,H.Dziubinska,E.Krol S
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292 R. Stahlberg, R.E. Cleland, E.
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310 E.Davies,B.Stankovic It is assu
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312 E.Davies,B.Stankovic 21.2 Evide
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314 E.Davies,B.Stankovic Fig.21.3.
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316 E.Davies,B.Stankovic Relative m
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318 E.Davies,B.Stankovic 1992; Beel
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320 E.Davies,B.Stankovic Hentze MW,
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322 J. Fromm, S. Lautner in the ran
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324 J. Fromm, S. Lautner cells (Sam
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326 J. Fromm, S. Lautner 22.5 Ion C
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328 J. Fromm, S. Lautner hastobedon
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330 J. Fromm, S. Lautner Beilby MJ,
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332 J. Fromm, S. Lautner Williams S
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334 S. Mancuso, S. Mugnai like the
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336 S. Mancuso, S. Mugnai 2,000 nM
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338 S. Mancuso, S. Mugnai the fourt
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340 S. Mancuso, S. Mugnai “slow-w
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342 S. Mancuso, S. Mugnai 23.6 Airb
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344 S. Mancuso, S. Mugnai that tree
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346 S. Mancuso, S. Mugnai Fort C, F
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348 S. Mancuso, S. Mugnai Pophof B,
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24 Electrophysiology and Phototropi
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370 E. Wagner et al. Table 25.1. Fl
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372 E. Wagner et al. Exudation [µl
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374 E. Wagner et al. metabolism at
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376 E. Wagner et al. The circadian
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378 E. Wagner et al. Fig.25.5. Time
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380 E. Wagner et al. Fig.25.7. Patt
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382 E. Wagner et al. Fig.25.9. Time
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384 E. Wagner et al. Fig.25.11. a K
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386 E. Wagner et al. 25.9 Conclusio
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388 E. Wagner et al. Lecharny A, Wa
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26 Signals and Signalling Pathways
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404 L.G. Perry et al. properties (S
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406 L.G. Perry et al. Fig.27.1. A s
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408 L.G. Perry et al. phytotoxins i
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410 L.G. Perry et al. monooxygenase
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412 L.G. Perry et al. 27.4 (±)-Cat
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414 L.G. Perry et al. (±)-catechin
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416 L.G. Perry et al. mineralizatio
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418 L.G. Perry et al. Dyer AR (2004
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420 L.G. Perry et al. Singh HP, Bat
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422 V.Ninkovic,R.Glinwood,J.Petters
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436 Subject Index defense 67, 95-10
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438 Subject Index sieve-tube-elemen
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