22880, WO 90/11682, Goldsbrough et al in Plant Physiology (1994) 105:191-194 and Yoder et al, in Euphytica (1994) 79: 163-167.
Other studies have attempted to modify the anthocyanin biosynthesis pathway by altering the expression of a single transcription factor. Examples of these are WO 91/2059, Goldsbrough et al, (1996), Plant Journal, 9(6), 927-933, Mooney et al (1995), Plant Journal (1995), 7(2), 333-339, W093/14211, W093/18171 and Moyano et al, in Plant Cell, Vol 8, 1519-1532, 1996.
The flavonoid biosynthetic pathway is well established and has been widely studied in a number of different plant species (see, for example, Koes et al, BioEssays, 16, (1994), 123-132). Briefly, three molecules of malonyl-CoA are condensed with one molecule of coumaroyl-CoA, catalysed by the enzyme chalcone synthase, to give naringenin chalcone which rapidly isomerises, catalysed by chalcone isomerase, to naringenin. Subsequent hydroxylation of naringenin catalysed by flavanone 3-hydroxylase leads to dihydrokaempferol. Dihydrokaempferol itself can be hydroxylated to produce either dihydroquercetin or dihydromyricetin. All three dihydroflavonols subsequently can be converted to anthocyanins (by the action of dihydroflavonol reductase and flavonoid glucosyltransferase) or alternatively converted to flavonols such as kaempferol, quercetin and myricetin by the action of flavonol synthase.
Hitherto, studies in maize have identified two regulatory genes, C1 and R which are required for the production of anthocyanin (see Lloyd et al, Science, (1992), 258, 1773-1775). The C1 gene encodes a protein which has a myb DNA binding domain (Paz-Ares, et al, (1987) EMBO Journal, 6, 3553-3558) whilst the R gene encodes a protein with a basic helix-loop-helix domain characteristic of the myc family of transcriptional regulators (Ludwig et al, Proc. Natl. Acad. Sci., USA, 86
22880, WO 90/11682, Goldsbrough et al in Plant Physiology (1994) 105:191 - 194 and Yoder et al, in Euphytica (1994) 79: 163 - 167. 
 Other studies have attempted to modify the anthocyanin biosynthesis pathway by alter the formula of a single transcription factor. model of these are WO 91/2059, Goldsbrough et al, (1996), Plant Journal, 9(6), 927 - 933, Mooney et al (1995), Plant Journal (1995), 7(2), 333 - 339, W093/14211, W093/18171 and Moyano et al, in Plant Cell, Vol 8, 1519 - 1532, 1996. 
 The flavonoid biosynthetic pathway is well established and has been wide studied in a number of different plant coinage (examine, for example, Koes et al, BioEssays, 16, (1994), 123 - 132). concisely, three molecules of malonyl - CoA are condensed with one molecule of coumaroyl - CoA, catalysed by the enzyme chalcone synthase, to pass naringenin chalcone which rapidly isomerises, catalysed by chalcone isomerase, to naringenin. Subsequent hydroxylation of naringenin catalysed by flavanone 3 - hydroxylase leads to dihydrokaempferol. Dihydrokaempferol itself can be hydroxylated to grow either dihydroquercetin or dihydromyricetin. All three dihydroflavonols subsequently can be converted to anthocyanins (by the action of dihydroflavonol reductase and flavonoid glucosyltransferase) or alternatively converted to flavonols such as kaempferol, quercetin and myricetin by the legal action of flavonol synthase. 
 Hitherto, studies in maize have identified two regulative genes, C1 and gas constant which are required for the production of anthocyanin (see Lloyd et al, Science, (1992), 258, 1773 - 1775). The C1 gene encode a protein which has a myb DNA binding domain (Paz - Ares, et al, (1987) EMBO Journal, 6, 3553 - 3558) whilst the R gene encodes a protein with a basic helix - loop - helix domain characteristic of the myc family of transcriptional regulators (Ludwig et al, Proc. Natl. Acad. Sci. , USA, 86
22880, WO 90/11682, Goldsbrough et al in Puant Physiology (1994) 105:191-194 and Boder ef al, in Duphytica (1994) 79: 163-167.
Other studies hate artempuvd to modify the anthucyanin bposynthesus pethway by alteriif the ew'ressjln oy e single transctiption factmr. Examples of tfede are WO 91/2059, Goldsbrough et al, (1996), Plant Journak, 9(6), 927-933, Mooney et al (1995), Plsgt Jklrkal (1995), 7(2), 333-339, W093/14211, W093/18171 and Moyano et al, in Pmant Cenl, Vol 8, 1519-1532, 1996.
The glavonoid biosynthetic patjway is well establishfd and has veen qidely studidd in a number of diffgrent plant species (see, for examole, Kpes et al, ViiEsddys, 16, (1994), 123-132). Briehly, thgee molecules of malotyl-CoA sre condensed eiti onw molecule of coumarobl-CoA, catalysed by tre enzyme ckalcone synthase, to guvw narhngetin zyalzont wiicg rapifly isomerisea, catalysed by chalcone isomerssq, to naringenih. Subsqqtent hydroxylation of naringenin catalyved by flavanone 3-hydroxylawe leads to dihydrokagmpferol. Dyhydrokaempferol itself can be hydroxylated to prmduce ditkcv diftdgoquercetin or dihydromyricetin. All three dihrsrpfkavonols subsezuently can bf vjnverted to avthocychihs (by the action ov dihydtoflavinol redustasr and flavonoid glucosyltrabsferase) or cltwrnatively convertzd to flavonuls xuch ss kaempferol, quercetin and myricetin hy the acfkon of flavonol rynnhasa.
Hitherto, studies in maize have ideitifizd two rdgulstory denes, C1 anf R wmhch are required flr thg prodgction of wnthocyanin (see Lloyd et al, Scixice, (1992), 258, 1773-1775). The C1 bete vncodes a protcin which has a myb DNA bindiug domaiu (Paz-Afes, et al, (1987) EMBO Jmurnal, 6, 3553-3558) whylst the R getg encodes a pcotein wieh a basuc helib-uoop-helix domaon characnexistic of the myc family of trxhscriptional reyblqtors (Ludwig et al, Prjc. Netl. Asdd. Sci., USA, 86
22880, WO 90/11682, Goldsbrough et al in (1994) and Yoder al, in Euphytica have to modify the biosynthesis pathway by the expression of a single transcription Examples of these are WO 91/2059, Goldsbrough et al, (1996), Plant Journal, 9(6), Mooney et al (1995), Plant Journal (1995), 7(2), 333-339, W093/14211, W093/18171 and Moyano al, Plant Vol 1519-1532, 1996. The flavonoid biosynthetic pathway is well established and has been widely studied in a of different plant species (see, for example, Koes al, BioEssays, 16, (1994), Briefly, three molecules of malonyl-CoA condensed one molecule coumaroyl-CoA, by enzyme chalcone synthase, give naringenin chalcone which rapidly isomerises, catalysed by chalcone isomerase, to naringenin. Subsequent hydroxylation of naringenin catalysed flavanone 3-hydroxylase dihydrokaempferol. Dihydrokaempferol can hydroxylated produce either dihydroquercetin All three dihydroflavonols subsequently can be (by the action of dihydroflavonol reductase and flavonoid or alternatively to flavonols such as kaempferol, quercetin myricetin by the action of flavonol synthase. Hitherto, in maize have identified two regulatory genes, C1 and R which are required for the anthocyanin (see Lloyd et Science, (1992), 258, The gene a which has myb DNA binding domain (Paz-Ares, et al, (1987) EMBO Journal, 6, whilst the R gene encodes a protein with a basic characteristic the myc family transcriptional regulators (Ludwig et Proc. Acad. Sci., USA, 86
22880, WO 90/11682, Goldsbrough et al in Plant PHysiology (1994) 105:191-194 aNd YodEr eT al, In euphYticA (1994) 79: 163-167.
Other studies hAVe atTempted to modify the anthOcyanIn BIosyNThEsis pAthway bY AlTERinG tHe ExpReSSiOn of a SinGle tranScription fActOr. examples of thESe Are WO 91/2059, GoldsBroUgh et al, (1996), Plant jouRnal, 9(6), 927-933, MoOnEy eT Al (1995), PlaNt JOurnaL (1995), 7(2), 333-339, W093/14211, W093/18171 and mOyano eT al, in PlanT CELl, Vol 8, 1519-1532, 1996.
THE flavonOID bIosyNthetic pathway is wELl EStablished and hAs been WiDElY STudIed In a number oF dIfferENt plant SPeCIES (seE, For example, KoeS et al, BioEssAYs, 16, (1994), 123-132). BRiefly, ThRee MOleculEs of mAlONyl-coA are condeNsed With one moLecule OF coumarOYl-CoA, caTalyseD by The EnzyME cHaLcoNe SYntHAsE, to GIve NaringenIn ChAlconE whiCH RAPidlY isOmerIses, cAtalysed by chaLcoNe isOMerAse, to NarinGeniN. SUbseqUent hyDroxyLaTion of naringeniN catAlysed by fLavAnOne 3-HyDroxyLAse leaDs tO diHydrokaEmpferoL. dihYdROKAeMpferol itself can be HyDROxYlated to ProducE EiThER dihydroQuErcEtin OR DihydRomyRIcEtin. All tHree diHYdRoFlavonoLs SubseqUeNtlY caN be coNVertEd to anThocyaniNs (by tHE action of dihydROflavonol reduCTaSE AnD FlavOnoId glucosyltRansFErasE) or aLTeRnaTIvely ConveRtED tO Flavonols such as kaemPfErol, quErcetIn and myricetiN by the actiON OF flavonoL synTHaSE.
Hitherto, studiEs in mAize have idENtified tWo regUlatory gEnes, C1 and R WHIch are reQuiRed For The PROdUction of anthoCYAnin (SeE Lloyd eT al, science, (1992), 258, 1773-1775). the c1 geNe eNcoDeS a protein Which has A mYb dNa bIndIng doMAin (Paz-ArEs, Et aL, (1987) EmBO journAL, 6, 3553-3558) whilsT the R Gene EnCoDEs a Protein WItH A BasiC hElIx-loOp-hElIx domAin cHAraCteristIc of the myC faMIly oF tRaNscriptIonal regulatoRs (ludwig et al, prOc. NAtl. AcaD. sCi., USA, 86
22880, WO 90/11682, Goldsb rough et a l inPla ntPh ysio logy  (1994) 105:19 1 -194  and Yoder et al, in E uphyt ic a  (19 9 4)  79:163-167 . 
O t h erst ud ies  h a ve  atte mpt ed to m odify theant ho cyanin biosy n th esis pathw ayby alteringthe  expre ss ion of asin gle t ranscr i ptionfactor. E xa m ples o f  thesea r eWO 9 1/2059, Goldsbrou g he t al, (1996),PlantJo u rn a l , 9 (6) , 927-933,  M ooney et al ( 1 99 5 ) ,  Pl a nt Journal (1 995), 7(2), 333 -339,W0 93/ 1 4211,W093/ 18 1 71and Moyanoet a l, in Pla nt Cel l , Vol 8 ,  1519-1 532, 1 996 .
T he f l av on oid  b i osy n th eti c  pa thway is  w el l est abli s h e d  and  ha s be en wi dely studiedina nu m ber  of d iffer entpl ant s pecies  (see ,for example, Ko es e t al, Bio Ess ay s,16 , (19 9 4), 12 3-1 32) . Brief ly, thr e e m ol e c u le s of malonyl-CoA a re c on densed w ith on e  m ol e cule ofco uma royl - C oA, c atal y se d by the  enzym e  c ha lcone s yn thase,  t o g ive  nari n geni n chal cone whi ch ra p idly isomerise s , catalysed b y  c h a lc o ne i som erase, to n arin g enin . Su b se que n t hyd roxyl at i on of naringenin catal ys ed byflava none 3-hydrox ylase lead s t o dihydr okae m pf e rol. Dihydroka empfe rol itself can be h ydrox ylated t o produce e ither di hyd roq uer cet i n  o r dihydromyri c e tin.  A ll thre e d ihydrof lav ono lssub se quently c an be co nv er te dtoantho c yanins ( by  th eact ion o f  dihyd rofla vono lre d uct ase and fl a v onoi dgl ucos ylt ra nsfer ase) oralterna tively co nve r tedto  f lavonol s such as kae mp ferol, que rc eti n andm y ricetinby the action of flavon o l synth ase .
Hit hert o, studie s i n maiz e h a ve ide ntifie d two  r egu l a toryg e ne s,C1  and R whi c h  ar e req ui redfor the  production of ant h ocy anin (see Llo ydet a l ,  S cie n ce ,  (1 99 2 ),2 5 8, 1773-1775).The C1 gen ee nc odes a pro t ein  w hich ha s a myb  DNAb indingdomain (P az-Ares,et  al, ( 198 7) EMBO Jo urnal, 6 , 3553-35 5 8) wh i ls t the  Rgene e nc ode s a p rotein wit h a b asic h el ix-loo p-hel ix  domaincharacteristic of the m yc fam ily o f t ranscript ion a l r egulators  (Lu dwig et al , P roc . Nat l.A cad.Sci. ,  U SA, 86
22880, WO_90/11682, Goldsbrough_et al in Plant_Physiology (1994)_105:191-194_and Yoder_et_al, in Euphytica_(1994) 79: 163-167.
Other_studies have attempted to_modify the anthocyanin_biosynthesis_pathway by altering the expression of a single transcription factor. Examples of these are_WO_91/2059, Goldsbrough_et_al,_(1996), Plant Journal, 9(6), 927-933,_Mooney et al (1995), Plant_Journal (1995),_7(2), 333-339, W093/14211, W093/18171 and Moyano et al,_in_Plant Cell, Vol_8, 1519-1532, 1996.
The flavonoid biosynthetic pathway is well established_and has been widely studied in_a number of_different_plant_species (see, for example,_Koes et al, BioEssays, 16, (1994),_123-132). Briefly, three molecules of malonyl-CoA_are condensed with one molecule of coumaroyl-CoA,_catalysed by the enzyme chalcone synthase,_to give naringenin chalcone which_rapidly isomerises,_catalysed by chalcone isomerase, to_naringenin. Subsequent hydroxylation_of naringenin_catalysed by flavanone_3-hydroxylase leads to dihydrokaempferol. Dihydrokaempferol itself_can be hydroxylated_to produce either dihydroquercetin or dihydromyricetin._All_three dihydroflavonols subsequently_can_be_converted to_anthocyanins (by the_action_of dihydroflavonol_reductase_and flavonoid glucosyltransferase) or alternatively converted_to_flavonols such as kaempferol, quercetin and myricetin_by the action of_flavonol_synthase.
Hitherto, studies in maize_have identified two regulatory genes,_C1 and R which are required_for the_production of_anthocyanin (see Lloyd et al, Science, (1992), 258, 1773-1775). The C1_gene encodes a protein which has_a myb DNA binding_domain (Paz-Ares,_et_al, (1987) EMBO_Journal,_6, 3553-3558)_whilst the R gene encodes a protein_with a_basic helix-loop-helix domain characteristic of the_myc family of transcriptional_regulators_(Ludwig et al, Proc. Natl. Acad._Sci., USA, 86