Additional file 1: of Protein analysis reveals differential accumulation of late embryogenesis abundant and storage proteins in seeds of wild and cultivated amaranth species
Creators: name: Esaú Bojórquez-Velázquez
name: Barrera-Pacheco, Alberto
name: Espitia-Rangel, Eduardo
name: Herrera-Estrella, Alfredo
name: Rosa, Ana Barba De La
Publisher: name: figshare
Year: 2019
Subjects: subject: Biophysics
subject: Biochemistry
subject: Microbiology
subject: FOS: Biological sciences
subject: FOS: Biological sciences
subject: Cell Biology
subject: Genetics
subject: Molecular Biology
subject: Evolutionary Biology
subject: 39999 Chemical Sciences not elsewhere classified
subject: FOS: Chemical sciences
subject: FOS: Chemical sciences
subject: Immunology
subject: FOS: Clinical medicine
subject: FOS: Clinical medicine
subject: 110309 Infectious Diseases
subject: FOS: Health sciences
subject: FOS: Health sciences
subject: Plant Biology

description: Figure S1. Triplicates of the 1D-SDS-PAGE of amaranth seed hydrophilic proteins. Each gel was obtained from an independent protein extraction. Lines: M, molecular weight marker; A, A. hybridus; B, A. powellii; C, A. cruentus cv Amaranteca; D, A. hypochondriacus cv Opaca (waxy); E, A. hypochondriacus cv Cristalina (non-waxy); F, A. hypochondriacus cv Nutrisol. Arrows at the right side indicate the differentially accumulated protein bands selected for nLC-MS/MS identification. Figure S2. Triplicates of the 1D-SDS-PAGE of amaranth seed hydrophobic proteins. Each gel was obtained from an independent protein extraction. Lines: M, molecular weight marker; A, A. hybridus; B, A. powellii; C, A. cruentus cv Amaranteca; D, A. hypochondriacus cv Opaca (waxy); E, A. hypochondriacus cv Cristalina (non-waxy); F, A. hypochondriacus cv Nutrisol. Arrows at the right side indicate the differentially accumulated protein bands selected for nLC-MS/MS identification. Figure S3. Clustal analysis of 11S globulins. Sequences Ah11SA (3QAC_A), Ah11SB (001411), Ah11SPheRich (006768), Ah11SHMW (021283), GmA1aB1b (1FXZ-A), GmA1bB2 (BAC55938.1), GmA2B1a (BAA00154.1), GmA3B4 (1OD5_A), GmA5A4B3 (BAD72975.1). Yellow squares: cysteine residues that form disulphide bonds between the acidic and basic subunits. Red squares: the proteolytic site for asparaginil endopeptidase that gives rise to the acid and basic subunits. Green squares: β-barrel domains. Figure S4. A) Representative diagram of the structural signature of the 11S globulins. The cysteines involved in the formation of the interchain disulfide bond are highly conserved. B) Cysteine contained in the acid subunit indicated in position 11. C) Cysteine contained in the basic subunit indicated in position 17. It can be observed that some amino acids are also conserved in the environment of the sequence of these cysteines, especially the site of proteolytic cleavage NG, five amino acids before the cysteine conserved in C). Figure S5. Amino acid composition of 11S globulins. Red squares indicate the percentage of phenylalanine. Figure S6. Ah11SHMW amino acid sequence. In green shows the cupin β-barrel domains of 11S globulins. The red and blue bold letters indicate the 9 repeated sequences that form the CTD-like domain and the alignment of this sequences are shown. Table S2. Late embryogenesis abundant proteins reported in the amaranth genome database. Table S3. Classification of amaranth 7S (vicilin) proteins according to the presence of specific structural domains. Proteins that were identified by LC-MS/MS in differentially accumulated bands are in bold red. (DOC 2265 kb)