PCMT1 / PIMT antibody Host rabbit
- Known as:
- PCMT1 / PIMT (anti-) Host host: rabbit
- Catalog number:
- 'ARP48668_T100
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- PCMT1 / PIMT antibody Host rabbit
Related genes to: PCMT1 / PIMT antibody Host rabbit
- Gene:
- PCMT1 NIH gene
- Name:
- protein-L-isoaspartate (D-aspartate) O-methyltransferase
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 6q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-09-11
- Date modifiied:
- 2017-11-27
- Gene:
- TGS1 NIH gene
- Name:
- trimethylguanosine synthase 1
- Previous symbol:
- NCOA6IP
- Synonyms:
- PIMT
- Chromosome:
- 8q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-19
- Date modifiied:
- 2016-10-05
Related products to: PCMT1 / PIMT antibody Host rabbit
Related articles to: PCMT1 / PIMT antibody Host rabbit
- Transcriptional coactivators play a crucial role in regulating gene expression. PRIP interacting protein with methyl transferase domain (PIMT)/trimethyl guanosine synthase 1 (TGS1) is a co-activator interacting protein with an RNA methyl transferase domain. PIMT serves as a bridge between HAT and non-HAT coactivators and differentially modulates gene expression. Disruption of PIMT is embryonic lethal. PIMT regulates hepatic gluconeogenesis and TNF-α-induced insulin resistance in the skeletal muscle. As a methyl transferase, PIMT controls post-transcriptional regulation of HIV-1 and is essential for human telomerase RNA biogenesis. This review comprehensively describes the dual role of PIMT, which promises to be a putative target in metabolic disorders. - Source: PubMed
Publication date: 2022/04/21
Edwin Rebecca KristinaChalla NagalakshmiSharma RahulSatyamoorthy KParsa KishoreMisra Parimal - We describe a novel Drosophila gene, dtl (Drosophila Tat-like), which encodes a 60-kDa protein with RNA binding activity and a methyltransferase (MTase) domain. Dtl has an essential role in Drosophila development. The homologs of DTL recently described include PIMT (peroxisome proliferator-activated receptor-interacting protein with a methyltransferase domain), an RNA-binding protein that interacts with and enhances the nuclear receptor coactivator function, and TGS1, the methyltransferase involved in the formation of the 2,2,7-trimethylguanosine (m3G) cap of non-coding small RNAs. DTL is expressed throughout all of the developmental stages of Drosophila. The dtl mRNA has two ORFs (uORF and dORF). The product of dORF is the 60-kDa PIMT/TGS1 homolog protein that is translated from an internal AUG located 538 bp downstream from the 5' end of the message. This product of dtl is responsible for the formation of the m3G cap of small RNAs of Drosophila. Trimethylguanosine synthase activity is essential in Drosophila. The deletion in the dORF or point mutation in the putative MTase active site results in a reduced pool of m3G cap-containing RNAs and lethality in the early pupa stage. The 5' region of the dtl message also has the coding capacity (uORF) for a 178 amino acid protein. For complete rescue of the lethal phenotype of dtl mutants, the presence of the entire dtl transcription unit is required. Transgenes that carry mutations within the uORF restore the MTase activity but result in only partial rescue of the lethal phenotype. Interestingly, two transgenes bearing a mutation in uORF or dORF in trans can result in complete rescue. - Source: PubMed
Publication date: 2005/01/31
Komonyi OrbánPápai GáborEnunlu IzzetMuratoglu SelenPankotai TiborKopitova DarijaMaróy PéterUdvardy AndorBoros Imre - A protein family including the recently identified PIMT/Tgs1 (PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase) was identified by searching databases for homologues of a newly identified Drosophila protein with RNA-binding activity and methyltransferase domain. Antibodies raised against a short peptide of the mammalian homologue show a 90-kDa isoform expressed specifically in rat brain and testis and a 55-kDa form expressed ubiquitously. In HeLa cells, the larger isoform of the protein is nuclear and associated with a 600-kDa complex, while the smaller isoform is mainly cytoplasmic and co-localizes to the tubulin network. Inhibition of PIMT/Tgs1 expression by siRNA in HeLa cells resulted in an increase in the percentage of cells in G2/M phases. In yeast two-hybrid and in vitro GST pull down experiments, the conserved C-terminal region of PIMT/Tgs1 interacted with the WD domain containing EED/WAIT-1 that acts as a polycomb-type repressor in the nucleus and also binds to integrins in the cytoplasm. Our experiments, together with earlier data, indicate that isoforms of the PIMT/Tgs1 protein with an RNA methyltransferase domain function both in the nucleus and in the cytoplasm and associate with both elements of the cytoskeletal network and nuclear factors known to be involved in gene regulation. - Source: PubMed
Enünlü IzzetPápai GáborCserpán ImreUdvardy AndorJeang Kuan-TehBoros Imre