Smyd1 is a SET and MYND domain-containing protein, which functions as a histone methyltransferase for control of gene expression and regulates the skeletal and cardiac muscle differentiation. In this study, the full-length cDNA sequences of Smyd1a and Smyd1b were cloned from Chinese perch, and their molecular structure and expression profile in response to nutrition supply and in vivo IGF treatments were also analyzed. The cDNA sequence of Smyd1a and Smyd1b consists of 1862 and 1802 base pairs (bp), encoding 479 and 476 amino acids, respectively. The SET domains of the two proteins were split into two segments by the MYND domain. Furthermore, the amino acid sequence of Smyd1a contains an extra 13-aa insertion in the SET domain in comparison with Smyd1b. The two genes apparently exhibited temporal and spatial differential expression status. In adults, the two genes showed the higher expression level in the muscle and heart than in other testing tissues. During the post-embryonic developmental stages, the higher expression of Smyd1a was detected at 150 days post-hatching (dph), whereas the expression of Smyd1b peaked at 50 dph. It was indicated that they have potential function in muscle developmental regulation. The mRNA levels of Smyd1a and Smyd1b were sharply up-regulated within one day after refeeding in the Chinese perch juveniles following fasting for a week. Moreover, IGF-1 treatments in vivo significantly stimulated their expression in the skeletal muscle. Together, these data provide us with further understanding of the molecular characterization and expression regulation of the two genes upon internal and external stimuli.
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http://dx.doi.org/10.1016/j.cbpb.2016.01.004 | DOI Listing |
Mol Cell Biol
November 2024
Department of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Smyd1, a member of the Smyd lysine methyltransferase family, plays an important role in myofibrillogenesis of skeletal and cardiac muscles. Loss of Smyd1b (a Smyd1 ortholog) function in zebrafish results in embryonic death from heart malfunction. encodes two isoforms, Smyd1b_tv1 and Smyd1b_tv2, differing by 13 amino acids due to alternative splicing.
View Article and Find Full Text PDFJ Genet Genomics
March 2021
Department of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, MD 21202, USA. Electronic address:
Skeletal and cardiac muscles are striated myofibers that contain highly organized sarcomeres for muscle contraction. Recent studies revealed that Smyd1, a lysine methyltransferase, plays a key role in sarcomere assembly in heart and trunk skeletal muscles. However, Smyd1 expression and function in craniofacial muscles are not known.
View Article and Find Full Text PDFFASEB J
May 2019
Department of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Two paralogues, and have been identified in zebrafish. Although Smyd1b function has been reported in fast muscle, its function in slow muscle and the function of Smyd1a, in general, are uncertain. In this study, we generated 2 mutant alleles and analyzed the muscle defects in and single and double mutants in zebrafish.
View Article and Find Full Text PDFComp Biochem Physiol B Biochem Mol Biol
September 2018
The Key Laboratory of Mariculture, Ministry of Education,Ocean University of China, 266003 Qingdao, China; Fisheries College, Ocean University of China, 266003 Qingdao, China. Electronic address:
Japanese flounder (Paralichthys olivaceus) undergoes metamorphosis by changing its body from the larval to the juvenile form, and this process involves muscle development. Smyd1, a histone methyltransferase, plays a role in the skeletal muscle. In the present study, the Smyd1a and Smyd1b expression patterns and their 5' UTR and exon 1 DNA methylation levels were analyzed during metamorphosis of the Japanese flounder.
View Article and Find Full Text PDFBiochem Biophys Res Commun
February 2018
Molecular Cardiology, Department of Inner Medicine II, University of Ulm, Ulm, Germany. Electronic address:
Sarcomeric protein turnover needs to be tightly balanced to assure proper assembly and renewal of sarcomeric units within muscle tissues. The mechanisms regulating these fundamental processes are only poorly understood, but of great clinical importance since many cardiac and skeletal muscle diseases are associated with defective sarcomeric organization. The SET- and MYND domain containing protein 1b (Smyd1b) is known to play a crucial role in myofibrillogenesis by functionally interacting with the myosin chaperones Unc45b and Hsp90α1.
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