Progress in controlling starch structure by modifying starch-branching enzymes
- 1.6k Downloads
This paper reviews the progress of development of plants with desirable starch structure by modifying starch branching enzymes. Starch-branching enzyme (SBE) is responsible for the creation of branches during starch biosynthesis in plastids, and is a major determinant of the final fine structure and physical properties of the starch.
Multiple isoforms of SBE have been found in plants, with each playing a different role in amylopectin synthesis. Different methods have been used to develop desirable starch structures by modifying the SBE activity. These can involve changing its expression level (either up-regulation or down-regulation), genetically modifying the activity of the SBE itself, and varying the length of its transferred chains. Changing the activity and the transferred chain length of SBE has been less studied than changing the expression level of SBE in vivo. This article reviews and summarizes new tools for developing plants producing the next generation of starches.
KeywordsStarch-branching enzyme Starch structure Expression level Activity Transferred chain length
Fluorophore-assisted carbohydrate electrophoresis
High-performance anion-exchange chromatography
Nuclear magnetic resonance
Targeted induced local lesions in genome
We thank Dr. Alex Chi Wu for insightful discussion and Dr. Mitchell A. Sullivan for manuscript review. We gratefully acknowledge the support of the 1000-Talents Program of the Chinese Foreign Experts Bureau.
- Brust H, Lehmann T, D’Hulst C, Fettke J (2014) Analysis of the functional interaction of Arabidopsis starch synthase and branching enzyme isoforms reveals that the cooperative action of SSI and BEs results in glucans with polymodal chain length distribution similar to amylopectin. PLoS ONE 9:e102364PubMedPubMedCentralCrossRefGoogle Scholar
- Butardo VM, Fitzgerald MA, Bird AR, Gidley MJ, Flanagan BM, Larroque O, Resurreccion AP, Laidlaw HK, Jobling SA, Morell MK, Rahman S (2011) Impact of down-regulation of starch branching enzyme IIb in rice by artificial microRNA- and hairpin RNA-mediated RNA silencing. J Exp Bot 62:4927–4941PubMedPubMedCentralCrossRefGoogle Scholar
- Delrue B, Fontaine T, Routier F, Decq A, Wieruszeski JM, Vandenkoornhuyse N, Maddelein ML, Fournet B, Ball S (1992) Waxy Chlamydomonas-reinhardtii: monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin. J Bacteriol 174:3612–3620PubMedPubMedCentralGoogle Scholar
- Garwood DL, Shannon JC, Creech RG (1976) Starches of endosperms possessing different alleles at amylose-extender locus in Zea mays L. Cereal Chem 53:355–364Google Scholar
- Hazard B, Zhang XQ, Colasuonno P, Uauy C, Beckles DM, Dubcovsky J (2012) Induced mutations in the starch branching enzyme II (SBEII) genes increase amylose and resistant starch content in durum wheat. Crop Sci 52:1754–1766Google Scholar
- Jespersen HM, Macgregor EA, Henrissat B, Sierks MR, Svensson B (1993) Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (β/α)(8)-barrel domain and evolutionary relationship to other amylolytic enzymes. J Protein Chem 12:791–805PubMedCrossRefGoogle Scholar
- Jobling SA, Schwall GP, Westcott RJ, Sidebottom CM, Debet M, Gidley MJ, Jeffcoat R, Safford R (1999) A minor form of starch branching enzyme in potato (Solanum tuberosum L.) tubers has a major effect on starch structure: cloning and characterisation of multiple forms of SBE A. Plant J. 18:163–171PubMedCrossRefGoogle Scholar
- Maddelein ML, Libessart N, Bellanger F, Delrue B, Dhulst C, Vandenkoornhuyse N, Fontaine T, Wieruszeski JM, Decq A, Ball S (1994) Toward an understanding of the biogenesis of the starch granule: determination of granule-bound and soluble starch synthase functions in amylopectin synthesis. J Biol Chem 269:25150–25157PubMedGoogle Scholar
- Makhmoudova A, Williams D, Brewer D, Massey S, Patterson J, Silva A, Vassall KA, Liu F, Subedi S, Harauz G, Siu KW, Tetlow IJ, Emes MJ (2014) Identification of multiple phosphorylation sites on maize endosperm starch branching enzyme IIb, a key enzyme in amylopectin biosynthesis. J Biol Chem 289:9233–9246PubMedPubMedCentralCrossRefGoogle Scholar
- Pal K, Kumar S, Sharma S, Garg SK, Alam MS, Xu HE, Agrawal P, Swaminathan K (2010) Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal beta-sandwich in substrate specificity and enzymatic activity. J Biol Chem 285:20897–20903PubMedPubMedCentralCrossRefGoogle Scholar
- Rahman S, Regina A, Li Z, Mukai Y, Yamamoto M, Kosar-Hashemi B, Abrahams S, Morell MK (2001) Comparison of starch-branching enzyme genes reveals evolutionary relationships among isoforms. Characterization of a gene for starch-branching enzyme IIa from the wheat D genome donor Aegilops tauschii (vol 125, pg 1314, 2001). Plant Physiol 126:463Google Scholar
- Santos CR, Tonoli CCC, Trindade DM, Betzel C, Takata H, Kuriki T, Kanai T, Imanaka T, Arni RK, Murakami MT (2011) Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Proteins-Struct Funct Bioinform 79:547–557CrossRefGoogle Scholar
- Yamanouchi H, Nakamura Y (1992) Organ specificity of isoforms of starch branching enzyme (Q-enzyme) in rice. Plant Cell Physiol 33:985–991Google Scholar
- Yao Y, Thompson DB, Guiltinan MJ (2004) Maize starch-branching enzyme isoforms and amylopectin structure. In the absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching. Plant Physiol 136:3515–3523PubMedPubMedCentralCrossRefGoogle Scholar