Abstract
The plant SABATH gene family is a group of O-methyltransferases (O-MTs), which belongs to the S-adenosyl-l-methionine-dependent methyltransferases (SAM-MTs). The resulting reaction products of SABATH genes play an important role in various processes of plant development. In this study, a total of 30 SABATH genes were detected in Salvia miltiorrhiza, which is an important medicinal plant, widely used to treat cardiovascular disease. Multiple sequence alignment and phylogenetic analyses showed that SmSABATH genes could be classified into three groups. The ratios of non-synonymous (Ka) and synonymous (Ks) substitution rates of 11 pairs paralogous of SmSABATH genes revealed that the SmSABATH genes had gone through purifying selection. Positive selection analyses using site models and branch-site models indicated that SmSABATH genes had undergone selective pressure for adaptive evolution. Functional divergence analyses suggested that the SmSABATH subgroup genes were divergent in terms of functions and positive selection sites that contributed to a functional divergence among the subgroups that were detected. Tissue-specific expression showed that the SABATH gene family in S. miltiorrhiza was primarily expressed in stems and leaves.
Highlights
Methylation is a ubiquitous reaction that takes place in bacteria, fungi, plants, and mammals.The process of methylation is catalyzed by S-adenosyl-L-methionine-dependent methyltransferases (SAM-MTs), and involves the transfer of the methyl group of S-adenosyl-L-methionine (SAM) to carbon, nitrogen, oxygen, or sulfur atoms, and modifies DNA, RNA, proteins, or small molecules with the formation of corresponding methylated products and S-adenosyl-L-homocysteine (SAH) [1].Enzymatic methylation of hydroxyl and carboxyl moieties are catalyzed by O-methyltransferases (O-MTs) [2], of which there are three defined types, via protein X-ray crystallography [3,4,5]
Functional divergence analyses suggested that the SmSABATH subgroup genes were divergent in terms of functions and positive selection sites that contributed to a functional divergence among the subgroups that were detected
The molecular weights of the predicted proteins ranged from 20.01 kDa (SMil_00022020) to 47.70 kDa (SMil_00023670) (Table S3), and the theoretical isoelectric points were predicted to range from 5.03 (SMil_00021702) to 9.58 (SMil_00008156) (Table S3)
Summary
The process of methylation is catalyzed by S-adenosyl-L-methionine-dependent methyltransferases (SAM-MTs), and involves the transfer of the methyl group of S-adenosyl-L-methionine (SAM) to carbon, nitrogen, oxygen, or sulfur atoms, and modifies DNA, RNA, proteins, or small molecules with the formation of corresponding methylated products and S-adenosyl-L-homocysteine (SAH) [1]. Enzymatic methylation of hydroxyl and carboxyl moieties are catalyzed by O-methyltransferases (O-MTs) [2], of which there are three defined types, via protein X-ray crystallography [3,4,5]. O-MTs exclusively methylate oxygen atoms of the hydroxyl moieties of phenylpropanoid-based compounds [6] and type 2 O-MTs are specific to phenylpropanoid esters of the coenzyme A, and are found in all lignin-producing plants [3]. The jasmonic acid carboxyl methyltransferase (JMT) [11], indole-3-acetic acid carboxyl methyltransferase (IAMT) [12], farnesoic acid carboxyl methyltransferase (FAMT) [13], and gibberellic acid carboxyl methyltransferase (GAMT) [14], were first identified in Arabidopsis
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
