Sorghum CCoAOMT and CCoAOMT-like gene evolution, structure, expression and the role of conserved amino acids in protein activity

被引:24
作者
Rakoczy, M. [1 ]
Femiak, I. [1 ]
Alejska, M. [1 ]
Figlerowicz, M. [1 ]
Podkowinski, J. [1 ]
机构
[1] PAS, Inst Bioorgan Chem, Ul Noskowskiego 12-14, PL-61704 Poznan, Poland
关键词
Sorghum (Sorghum bicolor L.); CCoAOMT; Gene expression; Phylogeny; Protein structure; COENZYME-A; 3-O-METHYLTRANSFERASE; CAFFEOYL-COA; DEPENDENT O-METHYLTRANSFERASE; ADENOSYL-L-METHIONINE; LIGNIN BIOSYNTHESIS; DOWN-REGULATION; BIOCHEMICAL-CHARACTERIZATION; PHENYLPROPANOID METABOLISM; SUBSTRATE SPECIFICITIES; LIGNIFICATION;
D O I
10.1007/s00438-018-1441-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Sorghum is a crop plant that is grown for seeds, sucrose, forage and biofuel production. In all these applications, lignin is a superfluous component that decreases the efficiency of technological processes. Caffeoyl-coenzyme A O-methyltransferase (CCoAOMT) is an enzyme involved in monolignol synthesis that affects the efficiency of lignification and lignin composition. The sorghum genome harbors one CCoAOMT gene and six closely related CCoAOMT-like genes. The structures of four sorghum CCoAOMT-like enzymes suggest that these proteins might methylate caffeoyl coenzyme A and contribute to monolignol synthesis. In this study, two sorghum genes, CCoAOMT and one CCoAOMT-like, were found to be highly expressed in leaves, stems and immature seeds. The promoters of these genes possess clusters of transcription factor-binding sites specific for lignification, and this suggests that they are important for lignification. Phylogenetic analysis revealed that one sorghum CCoAOMT-like enzyme is closely related to ancestral cyanobacterial CCoAOMT-like proteins. The remaining CCoAOMT-like enzymes, including the one highly expressed in the leaves and stem, are closely related to CCoAOMT. Genes from these two groups possess different, evolutionarily conserved gene structures. The structure of the sorghum CCoAOMT-like protein from the ancestral clade was modeled and differences between enzymes from the two clades were analyzed. These results facilitate a better understanding of the evolution of genes involved in lignification, and provide valuable data for sorghum improvement through traditional breeding or molecular genetic techniques. The findings suggest that CCoAOMT-like genes might be recruited in lignification and raise questions of the frequency of such functional shifts.
引用
收藏
页码:1077 / 1089
页数:13
相关论文
共 67 条
[1]   Trends in lignin modification: a comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity [J].
Anterola, AM ;
Lewis, NG .
PHYTOCHEMISTRY, 2002, 61 (03) :221-294
[2]   The cell biology of lignification in higher plants [J].
Barros, Jaime ;
Serk, Henrik ;
Granlund, Irene ;
Pesquet, Edouard .
ANNALS OF BOTANY, 2015, 115 (07) :1053-1074
[3]   Lignification in Sugarcane: Biochemical Characterization, Gene Discovery, and Expression Analysis in Two Genotypes Contrasting for Lignin Content [J].
Bottcher, Alexandra ;
Cesarino, Igor ;
dos Santos, Adriana Brombini ;
Vicentini, Renato ;
Sampaio Mayer, Juliana Lischka ;
Vanholme, Ruben ;
Morreel, Kris ;
Goeminne, Geert ;
Magalhaes Silva Moura, Jullyana Cristina ;
Nobile, Paula Macedo ;
Carmello-Guerreiro, Sandra Maria ;
dos Anjos, Ivan Antonio ;
Creste, Silvana ;
Boerjan, Wout ;
de Andrade Landell, Marcos Guimaraes ;
Mazzafera, Paulo .
PLANT PHYSIOLOGY, 2013, 163 (04) :1539-1557
[4]   Insights into Land Plant Evolution Garnered from the Marchantia polymorpha Genome [J].
Bowman, John L. ;
Kohchi, Takayuki ;
Yamato, Katsuyuki T. ;
Jenkins, Jerry ;
Shu, Shengqiang ;
Ishizaki, Kimitsune ;
Yamaoka, Shohei ;
Nishihama, Ryuichi ;
Nakamura, Yasukazu ;
Berger, Frederic ;
Adam, Catherine ;
Aki, Shiori Sugamata ;
Althoff, Felix ;
Araki, Takashi ;
Arteaga-Vazquez, Mario A. ;
Balasubrmanian, Sureshkumar ;
Barry, Kerrie ;
Bauer, Diane ;
Boehm, Christian R. ;
Briginshaw, Liam ;
Caballero-Perez, Juan ;
Catarino, Bruno ;
Chen, Feng ;
Chiyoda, Shota ;
Chovatia, Mansi ;
Davies, Kevin M. ;
Delmans, Mihails ;
Demura, Taku ;
Dierschke, Tom ;
Dolan, Liam ;
Dorantes-Acosta, Ana E. ;
Eklund, D. Magnus ;
Florent, Stevie N. ;
Flores-Sandoval, Eduardo ;
Fujiyama, Asao ;
Fukuzawa, Hideya ;
Galik, Bence ;
Grimanelli, Daniel ;
Grimwood, Jane ;
Grossniklaus, Ueli ;
Hamada, Takahiro ;
Haseloff, Jim ;
Hetherington, Alexander J. ;
Higo, Asuka ;
Hirakawa, Yuki ;
Hundley, Hope N. ;
Ikeda, Yoko ;
Inoue, Keisuke ;
Inoue, Shin-Ichiro ;
Ishida, Sakiko .
CELL, 2017, 171 (02) :287-+
[5]   A catalytic triad - Lys-Asn-Asp - Is essential for the catalysis of the methyl transfer in plant cation-dependent O-methyltransferases [J].
Brandt, Wolfgang ;
Manke, Kerstin ;
Vogt, Thomas .
PHYTOCHEMISTRY, 2015, 113 :130-139
[6]   Sweet sorghum as a model system for bioenergy crops [J].
Calvino, Martin ;
Messing, Joachim .
CURRENT OPINION IN BIOTECHNOLOGY, 2012, 23 (03) :323-329
[7]   Maize and sorghum: genetic resources for bioenergy grasses [J].
Carpita, Nicholas C. ;
McCann, Maureen C. .
TRENDS IN PLANT SCIENCE, 2008, 13 (08) :415-420
[8]   The biosynthesis of monolignols: a "metabolic grid", or independent pathways to guaiacyl and syringyl units? [J].
Dixon, RA ;
Chen, F ;
Guo, DJ ;
Parvathi, K .
PHYTOCHEMISTRY, 2001, 57 (07) :1069-1084
[9]   Both caffeoyl Coenzyme A 3-O-methyltransferase 1 and caffeic acid O-methyltransferase 1 are involved in redundant functions for lignin, flavonoids and sinapoyl malate biosynthesis in Arabidopsis [J].
Do, Cao-Trung ;
Pollet, Brigitte ;
Thevenin, Johanne ;
Sibout, Richard ;
Denoue, Dominique ;
Barriere, Yves ;
Lapierre, Catherine ;
Jouanin, Lise .
PLANTA, 2007, 226 (05) :1117-1129
[10]   ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites [J].
Emanuelsson, O ;
Nielsen, H ;
Von Heijne, G .
PROTEIN SCIENCE, 1999, 8 (05) :978-984