Carbon Flux and Carbohydrate Gene Families in Pineapple
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The recently sequenced pineapple genome was used to identify and analyze some of the key gene families involved in carbohydrate biosynthesis, breakdown and modification. Gene products were grouped into glycosyltransferases (GT), glycoside hydrolases (GH), carbohydrate esterases (CE), and polysaccharide lyases (PL) based upon predicted catalytic activity. Non-catalytic carbohydrate-binding modules (CBM) and enzymes involved in lignification were also identified. The pineapple genes were compared with those from two and five monocot and eudicots species, respectively. The complement of pineapple sugar and cell wall metabolism genes is similar to that found in rice and sorghum, though the numbers of GTs and GHs is often fewer. This applies to a lesser extent to the genes involved in nucleotide-sugar interconversion, with both pineapple and papaya having a minimum complement. Interestingly, pineapple does not appear to contain mixed linkage β-glucan in its walls while possessing cellulose synthase-like (Csl), J and H genes. Pineapple and papaya have less than half the number of GT1 genes involved in small molecule glycosylation compared to Arabidopsis and tomato, and fewer members in GH families than Arabidopsis. The ratio of rice and sorghum to pineapple genes in GH families was more variable than in the case of GTs and it is unclear why pineapple GH gene numbers are so low. Rice, sorghum and pineapple have far fewer CE8, PL1 and GH28 genes related to pectin metabolism than most eudicots. The general lower number of cell wall genes in pineapple possibly reflects the absence of a genome duplication event. The data also suggests that pineapple straddles the boundary between grasses (family Poaceae) and eudicots in terms of genes involved in carbohydrate metabolism, which is also reflected in its cell wall composition.
KeywordsCarbohydrate metabolism Glycoside hydrolases Glycosyltransferases Oxidases Plant cell walls Starch Sucrose
This work was supported by the USDA National Institute of Food and Agriculture, Hawaii Hatch Project #862, managed by the College of Tropical Agriculture and Human Resources.
- Capita NC, Ralph J, McCann MC (2015) The call wall. P 45–110, In. Buchanan BB, Gruissem W, Jones RL (2015) Biochemistry and Molecular Biology of Plants, 2nd Edition, American Society of Plant Biologists (Rockville, MD), Wiley BlackwellGoogle Scholar
- Chen CC, Paull RE (2000) Sugar metabolism and pineapple fruit translucency. J Am Soc Hort Sci 125:558–562Google Scholar
- Emanuelsson O, Nielsen H, Brunak S, Von Heijne G (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300(4):1005–1016Google Scholar
- Hsieh YS, Harris PJ (2009) Xyloglucans of monocotyledons have diverse structures. Molecular Plant 2:943-965Google Scholar
- Keegstra K, Cavalier D (2010) Glycosyltransferases of the GT34 and GT37 Families. In: Ulvskov P (ed) Annual plant reviews: plant polysaccharides, biosynthesis and bioengineering, vol 41. Blackwell Publishing, Oxford, pp 235–249Google Scholar
- Madden TL, Tatusov RL, Zhang J (1996) Applications of network BLAST server. Methods Enzymol 266:131–141Google Scholar
- Paull RE, Lobo M (2012) Pineapple p333–357. In: Tropical and Subtropical Fruit Processing and Packaging, Siddiq M (ed). Wiley, Ames, Iowa, USAGoogle Scholar
- Sampedro J, Cosgrove DJ (2005) The expansin superfamily. Genome Biol 6:242Google Scholar
- Trethewey JA, Campbell LM, Harris PJ (2005) (1 → 3),(1 → 4)-ß-d-Glucans in the cell walls of the Poales (sensu lato): an immunogold labeling study using a monoclonal antibody. Amer J Botany 92:1660–1674.Google Scholar
- Willats WG, Orfila C, Limberg G, Buchholt HC, van Alebeek G-J WM, Voragen AGJ, et al. (2001) Modulation of the degree and pattern of methyl-esterification of pectic homogalacturonan in plant cell walls. Implications for pectin methyl esterase action, matrix properties, and cell adhesion. J Biol Chem 276:19404–19413CrossRefPubMedGoogle Scholar
- Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ (2006) Crystal structure and activities of EXPB1 (Zea mays), a beta-expansin and group-1 pollen allergen from maize Proc Natl Acad Sci USA 103:14664–14671Google Scholar