TY - JOUR A1 - Cencil, Ugo A1 - Nitschke, Felix A1 - Steup, Martin A1 - Minassian, Berge A. A1 - Colleoni, Christophe A1 - Ball, Steven G. T1 - Transition from glycogen to starch metabolism in Archaeplastida JF - Trends in plant science N2 - In this opinion article we propose a scenario detailing how two crucial components have evolved simultaneously to ensure the transition of glycogen to starch in the cytosol of the Archaeplastida last common ancestor: (i) the recruitment of an enzyme from intracellular Chlamydiae pathogens to facilitate crystallization of alpha-glucan chains; and (ii) the evolution of novel types of polysaccharide (de)phosphorylating enzymes from preexisting glycogen (de)phosphorylation host pathways to allow the turnover of such crystals. We speculate that the transition to starch benefitted Archaeplastida in three ways: more carbon could be packed into osmotically inert material; the host could resume control of carbon assimilation from the chlamydial pathogen that triggered plastid endosymbiosis; and cyanobacterial photosynthate export could be integrated in the emerging Archaeplastida. KW - evolution of plastids KW - starch and glycogen metabolism KW - polyglucan debranching reactions KW - starch and glycogen (de)phosphorylation KW - Chlamydia-like bacteria KW - Lafora disease Y1 - 2014 U6 - https://doi.org/10.1016/j.tplants.2013.08.004 SN - 1360-1385 VL - 19 IS - 1 SP - 18 EP - 28 PB - Elsevier CY - London ER - TY - JOUR A1 - Dauvillee, David A1 - Chochois, Vincent A1 - Steup, Martin A1 - Haebel, Sophie A1 - Eckermann, Nora A1 - Ritte, Gerhard A1 - Ral, Jean-Philippe A1 - Colleoni, Christophe A1 - Hicks, Glenn A1 - Wattebled, Fabrice A1 - Deschamps, Philippe A1 - Lienard, Luc A1 - Cournac, Laurent A1 - Putaux, Jean-Luc A1 - Dupeyre, Danielle A1 - Ball, Steven G. T1 - Plastidial phosphorylase is required for normal starch synthesis in Chlamydomonas reinhardtii JF - The plant journal N2 - Among the three distinct starch phosphorylase activities detected in Chlamydomonas reinhardtii, two distinct plastidial enzymes (PhoA and PhoB) are documented while a single extraplastidial form (PhoC) displays a higher affinity for glycogen as in vascular plants. The two plastidial phosphorylases are shown to function as homodimers containing two 91-kDa (PhoA) subunits and two 110-kDa (PhoB) subunits. Both lack the typical 80-amino-acid insertion found in the higher plant plastidial forms. PhoB is exquisitely sensitive to inhibition by ADP-glucose and has a low affinity for malto-oligosaccharides. PhoA is more similar to the higher plant plastidial phosphorylases: it is moderately sensitive to ADP-glucose inhibition and has a high affinity for unbranched malto-oligosaccharides. Molecular analysis establishes that STA4 encodes PhoB. Chlamydomonas reinhardtii strains carrying mutations at the STA4 locus display a significant decrease in amounts of starch during storage that correlates with the accumulation of abnormally shaped granules containing a modified amylopectin structure and a high amylose content. The wild-type phenotype could be rescued by reintroduction of the cloned wild-type genomic DNA, thereby demonstrating the involvement of phosphorylase in storage starch synthesis. KW - Chlamydomonas KW - starch KW - amylopectin KW - (glycogen) starch phosphorylase Y1 - 2006 U6 - https://doi.org/10.1111/j.1365-313X.2006.02870.x SN - 0960-7412 VL - 48 IS - 2 SP - 274 EP - 285 PB - Blackwell CY - Oxford ER - TY - JOUR A1 - Deschamps, Philippe A1 - Haferkamp, Ilka A1 - Dauvillee, David A1 - Haebel, Sophie A1 - Steup, Martin A1 - Buleon, Alain A1 - Putaux, Jean-Luc A1 - Colleoni, Christophe A1 - d'Hulst, Christophe A1 - Plancke, Charlotte A1 - Gould, Sven A1 - Maier, Uwe A1 - Neuhaus, Heinz Eckhard A1 - Ball, Steven G. T1 - Nature of the periplastidial pathway of starch synthesis in the cryptophyte Guillardia theta N2 - The nature of the periplastidial pathway of starch biosynthesis was investigated with the model cryptophyte Guillardia theta. The storage polysaccharide granules were shown to be composed of both amylose and amylopectin fractions with a chain length distribution and crystalline organization very similar to those of starch from green algae and land plants. Most starch granules displayed a shape consistent with biosynthesis occurring around the pyrenoid through the rhodoplast membranes. A protein with significant similarity to the amylose-synthesizing granule-bound starch syntbase 1 from green plants was found as the major polypeptide bound to the polysaccharide matrix. N-terminal sequencing of the mature protein proved that the precursor protein carries a nonfunctional transit peptide in its bipartite topogenic signal sequence which is cleaved without yielding transport of the enzyme across the two inner plastid membranes. The enzyme was shown to display similar affinities for ADP and UDP-glucose, while the V-max measured with UDP-glucose was twofold higher. The granule-bound starch synthase from Guillardia theta was demonstrated to be responsible for the synthesis of long glucan chains and therefore to be the functional equivalent of the amylose- synthesizing enzyme of green plants. Preliminary characterization of the starch pathway suggests that Guillardia theta utilizes a UDP-glucose-based pathway to synthesize starch Y1 - 2006 UR - http://ec.asm.org/ U6 - https://doi.org/10.1128/Ec.00380-05 SN - 1535-9778 ER - TY - JOUR A1 - Nakamura, Yasunori A1 - Steup, Martin A1 - Colleoni, Christophe A1 - Iglesias, Alberto A. A1 - Bao, Jinsong A1 - Fujita, Naoko A1 - Tetlow, Ian T1 - Molecular regulation of starch metabolism JF - Plant molecular biology : an international journal of fundamental research and genetic engineering Y1 - 2022 U6 - https://doi.org/10.1007/s11103-022-01253-0 SN - 0167-4412 SN - 1573-5028 VL - 108 IS - 4-5 SP - 289 EP - 290 PB - Springer CY - Dordrecht ER -