Structure, Activity, and Function of Protein Methyltransferases
Jeltsch, Albert (editor)
Dhayalan, Arunkumar (editor)
This collection of review articles describes the structure, function and mechanism of individual protein methyltransferase enzymes including protein lysine methyltransferases, protein arginine methyltransferases, and also the less abundant protein histidine methyltransferases and protein N-terminal end methyltransferases. The topics covered in the individual reviews include structural aspects (domain architecture, homologs and paralogs, and structure), biochemical properties (mechanism, sequence specificity, product specificity, regulation, and histone and non-histone substrates), cellular features (subcellular localization, expression patterns, cellular roles and function, biological effects of substrate protein methylation, connection to cell signaling pathways, and connection to chromatin regulation) and their role in diseases. This review book is a useful resource for scientists working on protein methylation and protein methyltransferases and those interested in joining this emerging research field.
Keywordsprotein lysine methylation; H3K9 methylation; PKMT; enzyme specificity; enzyme regulation; heterochromatin; protein post-translational modification; NSD3; WHSC1L1; structure and function; protein arginine methylation; PRMT7; epigenetics; cancer; immunity; pluripotency; SETDB1; methyltransferase; schizophrenia; Huntington’s disease; Rett syndrome; Prader–Willi syndrome; congenital heart diseases; inflammatory bowel disease; MLL2; structure; H3K4me3; chromatin regulation; disease; dystonia; NSD1; H3K36; SOTOS; NUP98-NSD1; AML; PRMT6; post-translational modification; H3R2me2a; SETD3; posttranslational modifications; protein histidine methylation; actin; polymerization; cytoskeleton; enteroviruses; oncogenesis; PRMT5; cardiovascular disease; neurodegenerative diseases; diabetes; inflammation; G9a; GLP; EHMT2; EHMT1; post translational modification; lysine methylation; N-terminal methylation; translation; eEF1A; METTL13; neuron; synapse; dendritic spine; actin cytoskeleton; GTPase; PRMT1; arginine methylation; H4R3 methylation; transcriptional regulation; cell signaling; DNA damage repair; PRMT2; SH3; SETMAR; Metnase; H3K36me2; Hsmar1; non-homologous end joining repair; NHEJ; transposase; transposable elements; histone; SET7/9; SETD7; lysine-specific methyltransferase (PKMT); cell proliferation; stress response; post-translational protein modification; n/a
Webshop linkhttps://mdpi.com/books/pdfview ...
Publication date and placeBasel, 2022
Research & information: general
Biology, life sciences