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Data highlight the importance of the catalytic activity of PIMT to mediate VEGF effects during endothelial cell migration and tube formation in angiogenesis.
Self-association of Tgs1p and its catalytic activity were prerequisite to bypass the requirement for its accessory factor Swm2p for efficient pre-rRNA processing and snRNA trimethylation.
PIMT was identified as a key player responsible for glycated low density lipoproteins induced vascular endothelial cell apoptosis.
isoforms of the PIMT/Tgs1 protein with an RNA methyltransferase domain function both in the nucleus and in the cytoplasm
The protein L-isoaspartyl (D-aspartyl) methyltransferase (PIMT) is an enzyme that recognizes and repairs the abnormal L-isoaspartyl residues in proteins.
The structure-function data highlight a strictly essential pi-cation interaction between Trp766 and the m(7)G base and a network of important enzymic contacts to the cap triphosphate via Lys646, Tyr771, Arg807, and Lys836.
Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation.
proteasome maturation constitutes a mechanism regulating Tgs1 function by generating Tgs1 species with different substrate specificities, subcellular localizations, and functions.
These results highlight that PIMT expression is regulated by ROS and could primarily act as an antioxidant enzyme.
present a biochemical characterization of the human Tgs1 guanine-N2 methyltransferase reaction and identify individual amino acids required for methyltransferase activity in vitro and in vivo
m(7)GpppA binds via its adenosine moiety to the structurally conserved adenosylmethionine-binding pocket. The m(7) guanosine is unbound. The crystallized TGS1 fragment is catalytically inactive, but a fragment that is 17 AAs longer exhibits activity.
The crystal structure of the substrate bound methyltransferase domain as well as mutagenesis studies provide insight into the catalytic mechanism of TGS1.
PIMT is expressed in all cells of the E3.5day blastocyst in the mouse.
Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation (By similarity).
CLL-associated antigen KW-2
, PRIP-interacting protein PIPMT
, PRIP-interacting protein with methyltransferase domain
, PRIP-interacting protein with methyltransferase motif
, cap-specific guanine-N2 methyltransferase
, hepatocellular carcinoma-associated antigen 137
, nuclear receptor coactivator 6 interacting protein
, nuclear receptor coactivator 6-interacting protein
, trimethylguanosine synthase
, trimethylguanosine synthase homolog
, LOW QUALITY PROTEIN: trimethylguanosine synthase