03575nas a2200301   4500008004100000245011300041210006900154260000800223300000800231490000600239520261200245653001202857653001502869653001702884653001102901653001102912653002602923653001302949653001402962653001902976653002302995653003403018653002403052100002503076700002103101700002203122856012903144       2007                        eng d00aPolyglutamine variation in a flowering time protein correlates with island age in a Hawaiian plant radiation0 aPolyglutamine variation in a flowering time protein correlates w  cJan  a1050 v73 aBACKGROUND: A controversial topic in evolutionary developmental biology is whether morphological diversification in natural populations can be driven by expansions and contractions of amino acid repeats in proteins. To promote adaptation, selection on protein length variation must overcome deleterious effects of multiple correlated traits (pleiotropy). Thus far, systems that demonstrate this capacity include only ancient or artificial morphological diversifications. The Hawaiian Islands, with their linear geological sequence, present a unique environment to study recent, natural radiations. We have focused our research on the Hawaiian endemic mints (Lamiaceae), a large and diverse lineage with paradoxically low genetic variation, in order to test whether a direct relationship between coding-sequence repeat diversity and morphological change can be observed in an actively evolving system. RESULTS: Here we show that in the Hawaiian mints, extensive polyglutamine (CAG codon repeat) polymorphism within a homolog of the pleiotropic flowering time protein and abscisic acid receptor FCA tracks the natural environmental cline of the island chain, consequent with island age, across a period of 5 million years. CAG expansions, perhaps following their natural tendency to elongate, are more frequent in colonists of recently-formed, nutrient-rich islands than in their forebears on older, nutrient-poor islands. Values for several quantitative morphological variables related to reproductive investment, known from Arabidopsis fca mutant studies, weakly though positively correlate with increasing glutamine tract length. Together with protein modeling of FCA, which indicates that longer polyglutamine tracts could induce suboptimally mobile functional domains, we suggest that CAG expansions may form slightly deleterious alleles (with respect to protein function) that become fixed in founder populations. CONCLUSION: In the Hawaiian mint FCA system, we infer that contraction of slightly deleterious CAG repeats occurred because of competition for resources along the natural environmental cline of the island chain. The observed geographical structure of FCA variation and its correlation with morphologies expected from Arabidopsis mutant studies may indicate that developmental pleiotropy played a role in the diversification of the mints. This discovery is important in that it concurs with other suggestions that repetitive amino acid motifs might provide a mechanism for driving morphological evolution, and that variation at such motifs might permit rapid tuning to environmental change.10aAlleles10aDNA: Plant10aGenes: Plant10aHawaii10aMentha10aMinisatellite Repeats10aPeptides10aPhylogeny10aPlant Proteins10aSelection: Genetic10aSequence Homology: Amino Acid10aSpecies Specificity1 aLindqvist, Charlotte1 aLaakkonen, Liisa1 aAlbert, Victor, A  uhttps://lamiaceae.myspecies.info/content/polyglutamine-variation-flowering-time-protein-correlates-island-age-hawaiian-plant02853nas a2200349   4500008004100000245018100041210006900222260000800291300001400299490000800313520161000321653001001931653002401941653002301965653002101988653002302009653002702032653004402059653003802103653002802141653001402169653001702183653001902200653001402219653002702233653003402260653001202294100003202306700001902338700001802357856012802375       2004                        eng d00aCloning, functional expression, and characterization of the raffinose oligosaccharide chain elongation enzyme, galactan:galactan galactosyltransferase, from common bugle leaves0 aCloning functional expression and characterization of the raffin  cApr  a1377–870 v1343 aGalactan:galactan galactosyltransferase (GGT) is a unique enzyme of the raffinose family oligosaccharide (RFO) biosynthetic pathway. It catalyzes the chain elongation of RFOs without using galactinol (alpha-galactosyl-myoinositol) by simply transferring a terminal alpha-galactosyl residue from one RFO molecule to another one. Here, we report the cloning and functional expression of a cDNA encoding GGT from leaves of the common bugle (Ajuga reptans), a winter-hardy long-chain RFO-storing Lamiaceae. The cDNA comprises an open reading frame of 1215 bp. Expression in tobacco (Nicotiana plumbaginifolia) protoplasts resulted in a functional recombinant protein, which showed GGT activity like the previously described purified, native GGT enzyme. At the amino acid level, GGT shows high homologies (>60%) to acid plant alpha-galactosidases of the family 27 of glycosylhydrolases. It is clearly distinct from the family 36 of glycosylhydrolases, which harbor galactinol-dependent raffinose and stachyose synthases as well as alkaline alpha-galactosidases. Physiological studies on the role of GGT confirmed that GGT plays a key role in RFO chain elongation and carbon storage. When excised leaves were exposed to chilling temperatures, levels of GGT transcripts, enzyme activities, and long-chain RFO concentrations increased concomitantly. On a whole-plant level, chilling temperatures induced GGT expression mainly in the roots and fully developed leaves, both known RFO storage organs of the common bugle, indicating an adaptation of the metabolism from active growth to transient storage in the cold.10aAjuga10aAmino Acid Sequence10aCloning: Molecular10aCold Temperature10aDNA: Complementary10aGalactosyltransferases10aGene Expression Regulation: Enzymologic10aGene Expression Regulation: Plant10aMolecular Sequence Data10aPhylogeny10aPlant Leaves10aPlant Proteins10aRaffinose10aSequence Analysis: DNA10aSequence Homology: Amino Acid10aTobacco1 aTapernoux-Lüthi, Esther, M1 aBöhm, Andreas1 aKeller, Felix  uhttps://lamiaceae.myspecies.info/content/cloning-functional-expression-and-characterization-raffinose-oligosaccharide-chain02487nas a2200289   4500008004100000245009000041210006900131260000800200300001300208490000700221520160500228653001601833653002701849653002501876653001001901653002001911653001401931653001901945653002401964653001301988100001202001700001402013700001502027700001302042700001402055856012802069       2004                        eng d00aAmino acids composition of Teucrium nutlet proteins and their systematic significance0 aAmino acids composition of Teucrium nutlet proteins and their sy  cOct  a615–210 v943 aBACKGROUND AND AIMS: Plant species are considered as a good source of dietary proteins, although the nutritional quality of proteins depends on their amino acid composition. In this work the protein content and amino acid composition of nutlets of 21 Teucrium taxa (Lamiaceae) from Spain were analysed and their nutritional quality was compared with the minimum values established by the Food and Agriculture Organization of the United Nations (FAO). In addition, the amino acid composition was evaluated as a chemical character to clarify the taxonomic complexity in this genus. METHODS: Amino acid content of nutlets was determined after derivatization with diethyl ethoxymethylenemalonate by high-performance liquid chromatography. Previously, nutlets samples were hydrolysed and incubated in an oven at 110 degrees C for 24 h. KEY RESULTS: The protein content was variable, ranging from 6.4 % in T. dunense to 43.8 % in T. algarbiense. According to the FAO values all taxa contain satisfactory amounts of leucine, threonine and valine and are deficient in lysine. The similarity analysis of Teucrium taxa using amino acid composition data did not clearly reflect the infrageneric classification of this genus. CONCLUSIONS: Annual species, such as T. spinosum, T. aristatum and T. resupinatum showed a better balanced amino acid composition. The dendrogram partly matched with the karyological complexity of Teucrium. No correlation between amino acid composition and habitat has been observed, showing that Teucrium nutlet amino acid composition may not be strongly influenced by the environment.10aAmino Acids10aAmino Acids: Essential10aEvolution: Molecular10aFruit10aNutritive Value10aPhylogeny10aPlant Proteins10aSpecies Specificity10aTeucrium1 aJuan, R1 aPastor, J1 aMillán, F1 aAlaiz, M1 aVioque, J  uhttps://lamiaceae.myspecies.info/content/amino-acids-composition-teucrium-nutlet-proteins-and-their-systematic-significance03028nas a2200301   4500008004100000245013500041210006900176260000800245300001300253490000800266520210300274653001802377653002102395653001402416653001802430653002202448653001302470653002702483653001202510653001402522653001902536653002402555653003102579653001002610100002602620700002302646856005702669       2007                        eng d00aPopulation genetic structure and hybridization patterns in the Mediterranean endemics Phlomis lychnitis and P. crinita (Lamiaceae)0 aPopulation genetic structure and hybridization patterns in the M  cOct  a735–460 v1003 aBACKGROUND AND AIMS: The historical influence of gene flow and genetic drift after the last glacial phase of the Quaternary Period is reflected in current levels of genetic diversity and population structure of plant species. Moreover, hybridization after secondary contact might also affect population genetic diversity and structure. An assessment was made of the genetic variation and hybrid zone structure in Iberian populations of the Mediterranean Phlomis lychnitis and P. crinita, for which phylogenetic relationships are controversial, and hybridization and introgression are common. METHODS: Allozyme variation at 13 loci was analysed in 1723 individual plants sampled from 35 natural locations of P. lychnitis, P. crinita subsp. malacitana and P. crinita subsp. crinita in southern and eastern Spain. Standard genetic diversity parameters were calculated and patterns of genetic structure in each taxon were tested to fit the equilibrium between gene flow and genetic drift. Individual multilocus genotypes were subjected to Bayesian clustering analysis to estimate hybridization and introgression rates for both geographic regions. KEY RESULTS: Contrasting patterns in the distribution of genetic variation among the three taxa were found. Phlomis lychnitis showed no significant inbreeding, low genetic differentiation among populations and no evidence of isolation by distance. Phlomis crinita subsp. malacitana and P. crinita subsp. crinita showed high levels of genetic structure consistent with a pattern of gene flow-drift equilibrium. Higher instances of hybridization and introgression were detected in locations from southern Spain compared with locations from eastern Spain, matching unimodal and bimodal hybrid zones, respectively. CONCLUSIONS: High instances of historical gene flow, range expansion and altitudinal movement during the Quaternary Period, and lineage sorting can explain the diversity of patterns observed. The results suggest that P. lychnitis is the most differentiated lineage in the group; however, the relationship between the three taxa remains unclear.10aBayes Theorem10aCluster Analysis10aGene Flow10aGenetic Drift10aGenetic Variation10aGenotype10aHybridization: Genetic10aPhlomis10aPhylogeny10aPlant Proteins10aPopulation Dynamics10aSequence Analysis: Protein10aSpain1 aAlbaladejo, Rafael, G1 aAparicio, Abelardo  uhttp://aob.oxfordjournals.org/content/100/4/735.long02172nas a2200421   4500008004100000245014700041210006900188260000800257300001300265490000800278520081200286653001301098653001801111653002001129653001501149653002301164653001801187653003501205653001301240653002301253653002001276653003001296653001701326653003001343653002801373653001401401653003201415653002201447653001401469653001901483653001901502100002101521700001901542700001901561700002001580700002101600856012901621       2002                        eng d00aCYP98A6 from Lithospermum erythrorhizon encodes 4-coumaroyl-4'-hydroxyphenyllactic acid 3-hydroxylase involved in rosmarinic acid biosynthesis0 aCYP98A6 from Lithospermum erythrorhizon encodes 4coumaroyl4hydro  cMar  a219–240 v5143 aRosmarinic acid is the dominant hydroxycinnamic acid ester accumulated in Boraginaceae and Lamiaceae plants. A cytochrome P450 cDNA was isolated by differential display from cultured cells of Lithospermum erythrorhizon, and the gene product was designated CYP98A6 based on the deduced amino acid sequence. After expression in yeast, the P450 was shown to catalyze the 3-hydroxylation of 4-coumaroyl-4'-hydroxyphenyllactic acid, one of the final two steps leading to rosmarinic acid. The expression level of CYP98A6 is dramatically increased by addition of yeast extract or methyl jasmonate to L. erythrorhizon cells, and its expression pattern reflected the elicitor-induced change in rosmarinic acid production, indicating that CYP98A6 plays an important role in regulation of rosmarinic acid biosynthesis.10aAcetates10aCell Extracts10aCells: Cultured10aCinnamates10aCloning: Molecular10aCyclopentanes10aCytochrome P-450 Enzyme System10aDepsides10aDNA: Complementary10aGene Expression10aGene Expression Profiling10aLithospermum10aMixed Function Oxygenases10aMolecular Sequence Data10aOxylipins10aPhenylalanine Ammonia-Lyase10aPhenylpropionates10aPhylogeny10aPlant Proteins10aRNA: Messenger1 aMatsuno, Michiyo1 aNagatsu, Akito1 aOgihara, Yukio1 aEllis, Brian, E1 aMizukami, Hajime  uhttps://lamiaceae.myspecies.info/content/cyp98a6-lithospermum-erythrorhizon-encodes-4-coumaroyl-4-hydroxyphenyllactic-acid-302300nas a2200241   4500008004100000245016700041210006900208260000800277300001300285490000800298520143200306653001201738653003801750653001701788653001401805653001401819653001901833100001801852700002001870700002001890700001601910856013201926       2008                        eng d00aAltered expression patterns of TCP and MYB genes relating to the floral developmental transition from initial zygomorphy to actinomorphy in Bournea (Gesneriaceae)0 aAltered expression patterns of TCP and MYB genes relating to the  cJan  a532–430 v1783 aThe shift from zygomorphy to actinomorphy has been intensively studied in molecular genetic model organisms. However, it is still a key challenge to explain the great morphological diversity of derived actinomorphy in angiosperms, since different underlying mechanisms may be responsible for similar external morphologies. Bournea (Gesneriaceae) is of particular interest in addressing this question, as it is a representative of primarily derived actinomorphy characteristic of a unique developmental transition from zygomorphy to actinomorphic flowers at anthesis. Using RNA in situ hybridization, the expression patterns were investigated of three different Bournea orthologues of TCP and MYB genes that have been shown to control floral symmetry in model species. Here, it is shown that the initial zygomorphic pattern in Bournea is likely a residual zygomorphy resulting from conserved expression of the adaxial (dorsal) identity gene BlCYC1. As a key novel event, the late downregulation of BlCYC1 and BlRAD and the correlative changes in the late specific expression of the abaxial (ventral) identity gene BlDIV should be responsible for the origin of the derived actinomorphy in Bournea. These results further indicate that there might be diverse pathways in the origin and evolution of derived actinomorphy through modifications of pre-existing zygomorphic developmental programs under dynamics of regulatory networks.10aFlowers10aGene Expression Regulation: Plant10aGenes: Plant10aLamiaceae10aPhylogeny10aPlant Proteins1 aZhou, Xiu-Ren1 aWang, Yin-Zheng1 aSmith, James, F1 aChen, Rujin  uhttps://lamiaceae.myspecies.info/content/altered-expression-patterns-tcp-and-myb-genes-relating-floral-developmental-transition02990nas a2200445   4500008004100000245012100041210006900162260000800231300001400239490000700253520151700260653002401777653002301801653001501824653002501839653002801864653004101892653003001933653001301963653001601976653002301992653002202015653002802037653002402065653002102089653001402110653001902124653002102143653001502164653005202179653003402231653002602265100002002291700002402311700001802335700001802353700002202371700001902393856013202412       2007                        eng d00aEvolution of Cinnamate/p-coumarate carboxyl methyltransferases and their role in the biosynthesis of methylcinnamate0 aEvolution of Cinnamatepcoumarate carboxyl methyltransferases and  cOct  a3212–290 v193 aMethylcinnamate, which is widely distributed throughout the plant kingdom, is a significant component of many floral scents and an important signaling molecule between plants and insects. Comparison of an EST database obtained from the glandular trichomes of a basil (Ocimum basilicum) variety that produces high levels of methylcinnamate (line MC) with other varieties producing little or no methylcinnamate identified several very closely related genes belonging to the SABATH family of carboxyl methyltransferases that are highly and almost exclusively expressed in line MC. Biochemical characterization of the corresponding recombinant proteins showed that cinnamate and p-coumarate are their best substrates for methylation, thus designating these enzymes as cinnamate/p-coumarate carboxyl methyltransferases (CCMTs). Gene expression, enzyme activity, protein profiling, and metabolite content analyses demonstrated that CCMTs are responsible for the formation of methylcinnamate in sweet basil. A phylogenetic analysis of the entire SABATH family placed these CCMTs into a clade that includes indole-3-acetic acid carboxyl methyltransferases and a large number of uncharacterized carboxyl methyltransferase-like proteins from monocots and lower plants. Structural modeling and ligand docking suggested active site residues that appear to contribute to the substrate preference of CCMTs relative to other members of the SABATH family. Site-directed mutagenesis of specific residues confirmed these findings.10aAmino Acid Sequence10aBlotting: Southern10aCinnamates10aEvolution: Molecular10aExpressed Sequence Tags10aGas Chromatography-Mass Spectrometry10aGene Expression Profiling10aKinetics10aMethylation10aMethyltransferases10aModels: Molecular10aMolecular Sequence Data10aMolecular Structure10aOcimum basilicum10aPhylogeny10aPlant Proteins10aProtein Isoforms10aProteomics10aReverse Transcriptase Polymerase Chain Reaction10aSequence Homology: Amino Acid10aSubstrate Specificity1 aKapteyn, Jeremy1 aQualley, Anthony, V1 aXie, Zhengzhi1 aFridman, Eyal1 aDudareva, Natalia1 aGang, David, R  uhttps://lamiaceae.myspecies.info/content/evolution-cinnamatep-coumarate-carboxyl-methyltransferases-and-their-role-biosynthesis