Expression analyses of soluble starch synthase and starch branching enzyme isoforms in stem and leaf tissues under different photoperiods in lentil (Lens culinaris Medik.)

Biologia ◽  
2022 ◽  
Author(s):  
Yusuf C. Gercek ◽  
Kadir Boztas ◽  
Cihan Aydin ◽  
Hande Morgil ◽  
Ibrahim Baris ◽  
...  
Keyword(s):  
Lens Culinaris ◽  
Soluble Starch ◽  
Starch Synthase ◽  
Branching Enzyme ◽  
Starch Branching Enzyme ◽  
Enzyme Isoforms ◽  
Leaf Tissues

scholarly journals Differential Expression and Properties of Starch Branching Enzyme Isoforms in Developing Wheat Endosperm

1997 ◽  
Vol 113 (1) ◽  
pp. 201-208 ◽  
Author(s):  
M. K. Morell ◽  
A. Blennow ◽  
B. Kosar-Hashemi ◽  
M. S. Samuel
Keyword(s):  
Differential Expression ◽  
Branching Enzyme ◽  
Starch Branching Enzyme ◽  
Wheat Endosperm ◽  
Enzyme Isoforms

scholarly journals Differential Characteristics and Subcellular Localization of Two Starch-branching Enzyme Isoforms Encoded by a Single Gene inPhaseolus vulgaris L.

2002 ◽  
Vol 277 (19) ◽  
pp. 16538-16546 ◽  
Author(s):  
Shigeki Hamada ◽  
Hiroyuki Ito ◽  
Susumu Hiraga ◽  
Keisuke Inagaki ◽  
Kouichi Nozaki ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Single Gene ◽  
Branching Enzyme ◽  
Starch Branching Enzyme ◽  
Enzyme Isoforms

scholarly journals Soluble isoforms of starch synthase and starch-branching enzyme also occur within starch granules in developing pea embryos

1993 ◽  
Vol 4 (1) ◽  
pp. 191-198 ◽  
Author(s):  
Kay Denyer ◽  
Christopher Sidebottom ◽  
Christopher M. Hylton ◽  
Alison M. Smith
Keyword(s):  
Starch Synthase ◽  
Starch Granules ◽  
Branching Enzyme ◽  
Starch Branching Enzyme

Large-scale isolation, fractionation, and purification of soluble starch-synthesizing enzymes: starch synthase and branching enzyme from potato tubers

2010 ◽  
Vol 345 (11) ◽  
pp. 1555-1563 ◽  
Author(s):  
Rupendra Mukerjea ◽  
Daniel J. Falconer ◽  
Seung-Heon Yoon ◽  
John F. Robyt
Keyword(s):  
Large Scale ◽  
Soluble Starch ◽  
Starch Synthase ◽  
Potato Tubers ◽  
Branching Enzyme

Glucan affinity of starch synthase IIa determines binding of starch synthase I and starch-branching enzyme IIb to starch granules

2012 ◽  
Vol 448 (3) ◽  
pp. 373-387 ◽  
Author(s):  
Fushan Liu ◽  
Nadya Romanova ◽  
Elizabeth A. Lee ◽  
Regina Ahmed ◽  
Martin Evans ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Protein Interactions ◽  
Starch Granule ◽  
Protein Complexes ◽  
Starch Synthase ◽  
Starch Granules ◽  
Branching Enzyme ◽  
Wild Type ◽  
Protein Protein Interactions ◽  
Starch Branching Enzyme

The sugary-2 mutation in maize (Zea mays L.) is a result of the loss of catalytic activity of the endosperm-specific SS (starch synthase) IIa isoform causing major alterations to amylopectin architecture. The present study reports a biochemical and molecular analysis of an allelic variant of the sugary-2 mutation expressing a catalytically inactive form of SSIIa and sheds new light on its central role in protein–protein interactions and determination of the starch granule proteome. The mutant SSIIa revealed two amino acid substitutions, one being a highly conserved residue (Gly522→Arg) responsible for the loss of catalytic activity and the inability of the mutant SSIIa to bind to starch. Analysis of protein–protein interactions in sugary-2 amyloplasts revealed the same trimeric assembly of soluble SSI, SSIIa and SBE (starch-branching enzyme) IIb found in wild-type amyloplasts, but with greatly reduced activities of SSI and SBEIIb. Chemical cross-linking studies demonstrated that SSIIa is at the core of the complex, interacting with SSI and SBEIIb, which do not interact directly with each other. The sugary-2 mutant starch granules were devoid of amylopectin-synthesizing enzymes, despite the fact that the respective affinities of SSI and SBEIIb from sugary-2 for amylopectin were the same as observed in wild-type. The data support a model whereby granule-bound proteins involved in amylopectin synthesis are partitioned into the starch granule as a result of their association within protein complexes, and that SSIIa plays a crucial role in trafficking SSI and SBEIIb into the granule matrix.

Sign in / Sign up

Export Citation Format

Share Document