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Information on EC 2.1.1.296 - methyltransferase cap2
for references in articles please use BRENDA:EC2.1.1.296
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.296 methyltransferase cap2
IUBMB Comments
The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA]
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a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
Synonyms
hmtr2, cmtr2, ftsjd1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cap2
CMTr2
mRNA (nucleoside-2'-O)-methyltransferase
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ambiguous
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MTR2
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CMTr2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mRNA capping II
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-ribonucleotide-[mRNA] 2'-O-methyltransferase
The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
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Substrates: -
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
Substrates: -
Products: -
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
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Substrates: -
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
Substrates: -
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additional information
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Substrates: hMTr2 protein transfers a methyl group from S-adenosylmethionine to the 2'-O-ribose of the second nucleotide of messenger RNA and small nuclear RNA
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additional information
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Substrates: hMTr2 protein transfers a methyl group from S-adenosylmethionine to the 2'-O-ribose of the second nucleotide of messenger RNA and small nuclear RNA
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additional information
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Substrates: the recombinant enzyme produces a RNase T2-resistant RNA fragment, cap012, from cap01-RNA, but shows no activity with a purified BAP protein. Only a subset of labeled RNA molecules that has GpppG incorporated during transcription is a substrate for hMTr2. hMTr2 recognizes TMG-capped snRNAs in vitro
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additional information
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Substrates: the recombinant enzyme produces a RNase T2-resistant RNA fragment, cap012, from cap01-RNA, but shows no activity with a purified BAP protein. Only a subset of labeled RNA molecules that has GpppG incorporated during transcription is a substrate for hMTr2. hMTr2 recognizes TMG-capped snRNAs in vitro
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additional information
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Substrates: a conventional 5'-terminal structure of eukaryotic mRNAs consists of a 7-methylguanosine (m7G) moiety linked to the first transcribed nucleotide by a 5' to 5' triphosphate bridge resulting in the structure m7GpppN, which is referred to as cap 0, and most often the first and second transcribed nucleotide carry 2'-O-methyl groups (cap 1 and cap 2 structures, respectively). The cap2 methyltransferase, EC 2.1.1.296 transfers the methyl group to the second nucleotide. In contrast, four nucleotides adjacent to the m7G cap are methylated at the SL RNA 5' end to generate a cap 4 structure: m7G-ppp-N6,N6,2'-O-trimethyladenosine-p-2'-O-methyladenosine-p-2'-O-methylcytosine-p-N3,2'-O-methyluridine. The cap 4 structure seems to be restricted to the family Trypanosomatidae
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additional information
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Substrates: the enzyme builds the cap 4 structure, usage of an assay with digestion with ribonuclease T2, to monitor the presence of 2'-O-modifications at positions +1 to +4 of the SL sequence
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
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Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
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Substrates: -
Products: -
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additional information
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Substrates: hMTr2 protein transfers a methyl group from S-adenosylmethionine to the 2'-O-ribose of the second nucleotide of messenger RNA and small nuclear RNA
Products: -
Products: -
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additional information
?
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Substrates: hMTr2 protein transfers a methyl group from S-adenosylmethionine to the 2'-O-ribose of the second nucleotide of messenger RNA and small nuclear RNA
Products: -
Products: -
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additional information
?
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Substrates: a conventional 5'-terminal structure of eukaryotic mRNAs consists of a 7-methylguanosine (m7G) moiety linked to the first transcribed nucleotide by a 5' to 5' triphosphate bridge resulting in the structure m7GpppN, which is referred to as cap 0, and most often the first and second transcribed nucleotide carry 2'-O-methyl groups (cap 1 and cap 2 structures, respectively). The cap2 methyltransferase, EC 2.1.1.296 transfers the methyl group to the second nucleotide. In contrast, four nucleotides adjacent to the m7G cap are methylated at the SL RNA 5' end to generate a cap 4 structure: m7G-ppp-N6,N6,2'-O-trimethyladenosine-p-2'-O-methyladenosine-p-2'-O-methylcytosine-p-N3,2'-O-methyluridine. The cap 4 structure seems to be restricted to the family Trypanosomatidae
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
the N-terminal RFM domain has a conserved S-adenosyl-L-methionine-binding site (motifs I-III)
S-adenosyl-L-methionine
cofactor binding by CMTr2 is essential for the binding of RNA, residues K74, L77, W85, T89, K307, H142, and E145 are involved
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
neither N7 methylation of the guanosine cap nor 2'-O-ribose methylation of the first transcribed nucleotide are required for hMTr2, but the presence of cap1 methylation increases hMTr2 activity
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additional information
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neither N7 methylation of the guanosine cap nor 2'-O-ribose methylation of the first transcribed nucleotide are required for hMTr2, but the presence of cap1 methylation increases hMTr2 activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Distinct patterns of somatic genome alterations in lung adenocarcinomas and squamous cell carcinomas.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
localization of hMTr2 assayed in situ by immunostaining of epitope-tagged protein
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brenda
additional information
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localization of hMTr2 assayed in situ by immunostaining of epitope-tagged protein
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
the 5' cap of human messenger RNA contains 2'-O-methylation of the first and often second transcribed nucleotide that is important for its processing, translation and stability. Enzyme responsible for the methylations are CMTr1 and CMTr2, respectively
physiological function
additional information
evolution
the enzyme shows significant sequence and structural similarities to vaccinia virus VP39, another cap-specific RNA 2'-O-methyltransferase. TbMT48 or TbMT57 are two protein components of the cap 4 biosynthetic machinery
evolution
the enzyme belongs to the Rossmann-fold MTase (RFM) family, hMTr1 and hMTr2 are paralogues forming a subfamily with higher eukaryotic and viral members, minimum evolution tree of homologues of known 2'-O-ribose mRNA cap MTases, overview
evolution
MT57 homologs are only found in trypanosomatid protozoa that have a cap 4 structure and in poxviruses, of which vaccinia virus is a prototype, TbMT48 or TbMT57 are two protein components of the cap 4 biosynthetic machinery
malfunction
an observed defect in cap 4 modification is a specific effect of MT48 ablation
malfunction
downregulation by RNAi or genetic ablation of TbMT57 result in the accumulation of SL RNA missing 2'-O-methyl groups at positions +3 and +4 and thus bearing a cap 2 rather than a cap 4. Genetic ablation of MT57 results in viable cells with no apparent defect in SL RNA transsplicing, suggesting that MT57 is not essential or that trypanosomes have developed alternate mechanisms to counteract the absence of this protein
malfunction
the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity
malfunction
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enzyme-deficient mutant flies are viable and fertile as single and double mutants, exhibiting a slightly reduced survival to adulthood after hatching from the egg, and reduced climbing activity in negative geotaxis assays. In addition, isoform CMTr1 mutants, and to a greater extent isoform CMTr2 mutants, have reduced numbers of synapses at neuromuscular junctions of third instar larvae
physiological function
TbMT48 or TbMT57 are two protein components of the cap 4 biosynthetic machinery. The enzymes involved in cap 4 biogenesis, TbMT48 and TbMT57, are encoded by non-essential genes, considering that the SL cap 4 structure is a crucial determinant for trans-splicing competence of the SL RNA
physiological function
the 5' cap of human messenger RNA consists of an inverted 7-methylguanosine linked to the first transcribed nucleotide by a unique 5'-5' triphosphate bond followed by 2'-O-ribose methylation of the first and often the second transcribed nucleotides, likely serving to modify efficiency of transcript processing, translation and stability. Cap2 methylates the ribose of the second transcribed nucleotide. Relationship to other cap-modifying enzymes, overview
physiological function
the enzyme is involved in formation of the cap 4 structure, a cap structure of the SL RNA unique in eukaryotes with 4 nucleotides after the cap carrying a total of seven methyl groups. Modifications at the +3 and +4 positions are important for binding to the nuclear cap-binding complex, but MT57 is not essential. The Trypanosoma brucei cap binding complex can distinguish between a cap 4 and an m7G structure and it has a much higher affinity for the cap 4 substrate
physiological function
enzyme Cap2 expression is regulated by Pax6, a key regulator of the entire cascade of ocular lens formation through specific binding to promoters and enhancers of batteries of target genes
physiological function
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enzyme-mediated mRNA cap 2'-O-ribose methylation is required for reward learning in Drosophila
additional information
enzyme MT48 structural modeling using the VP39 crystal structure as a template, TbMT48 domains involved in S-adenosyl-methionine and cap binding, overview
additional information
FTSJD1, the candidate hMTr2, is composed of two RFM domains, sequence comparisons, and has a K-D-K active site. Each residue of the K-D-K triad is essential for the activity of the enzyme
additional information
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FTSJD1, the candidate hMTr2, is composed of two RFM domains, sequence comparisons, and has a K-D-K active site. Each residue of the K-D-K triad is essential for the activity of the enzyme
additional information
structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation, homology modeling of the CMTr2 catalytic domain bound to its target using the crystal structure of CMTr1 catalytic domain, overview. CMTr2 is divided into two parts: the amino-terminal part with the catalytic RFM domain (CMTr21-430) and the C-terminal part with the non-catalytic RFM domain (CMTr2430-770). The single domains of CMTr2 do not bind the substrate and do not exhibit any cap MTase activity alone or when mixed together as separately purified chains. Thus, CMTr2 requires both RFM domains in a single polypeptide chain for substrate binding and methylation. Residues K74, L77, W85, T89, K307, H142, and E145 are involved in RNA binding and catalysis, while residues residues S78, H86 and Q113 are not important
additional information
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structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation, homology modeling of the CMTr2 catalytic domain bound to its target using the crystal structure of CMTr1 catalytic domain, overview. CMTr2 is divided into two parts: the amino-terminal part with the catalytic RFM domain (CMTr21-430) and the C-terminal part with the non-catalytic RFM domain (CMTr2430-770). The single domains of CMTr2 do not bind the substrate and do not exhibit any cap MTase activity alone or when mixed together as separately purified chains. Thus, CMTr2 requires both RFM domains in a single polypeptide chain for substrate binding and methylation. Residues K74, L77, W85, T89, K307, H142, and E145 are involved in RNA binding and catalysis, while residues residues S78, H86 and Q113 are not important
Show AA Sequence and Transmembrane Helices (1432 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
CMTr2 is divided into two parts: the amino-terminal part with the catalytic RFM domain (CMTr21-430) and the C-terminal part with the non-catalytic RFM domain (CMTr2430-770). The single domains of CMTr2 do not bind the substrate and do not exhibit any cap MTase activity alone or when mixed together as separately purified chains. Thus, CMTr2 requires both RFM domains in a single polypeptide chain for substrate binding and methylation
additional information
-
CMTr2 is divided into two parts: the amino-terminal part with the catalytic RFM domain (CMTr21-430) and the C-terminal part with the non-catalytic RFM domain (CMTr2430-770). The single domains of CMTr2 do not bind the substrate and do not exhibit any cap MTase activity alone or when mixed together as separately purified chains. Thus, CMTr2 requires both RFM domains in a single polypeptide chain for substrate binding and methylation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E145A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
H142A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K307A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K74A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
L77A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
T89A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
W85A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K266A
site-directed mutagenesis, partly complements the enzyme defective mtant MT57-/- cells
W62D/G63D/Q64D
site-directed mutagenesis, partly complements the enzyme defective mtant MT57-/- cells
additional information
additional information
mutants of the K-D-K triad active site residues exchanged for alanine are all cataltyically inactive
additional information
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mutants of the K-D-K triad active site residues exchanged for alanine are all cataltyically inactive
additional information
the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity
additional information
-
the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity
additional information
silencing of TbMT48 mRNA by RNAi downregulation does not produce a lethal phenotype, as MT48-RNAi trypanosomes remain viable even after 10 days of tetracycline induction, generation of MT48 KO clonal cell lines by homologous recombination with PCR-generated cassettes. An observed defect in cap 4 modification, specific for MT48 ablation, can be complemented by reintroduction of a copy of the MT48 gene into mt48-/- cells
additional information
genetic ablation of MT57 is compatible with cell viability and leads to the accumulation of SL RNA with a cap structure defective at positions +3 and +4.. Transsplicing utilization of the SL RNA is not detectably affected in mt57-/- cells, analysis of the SL cap structure in mt57-/- cells, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CMTR2, recombinant overexpression of wild-type and mutant enzymes in HEK-293 cells
gene HMTR2 or FTSJD1, phylogenetic tree, functional overexpression of the cap2 MTase hMTr2 and of c-myc-tagged enzyme in MCF7 cells
primer extension analysis, functional expression observed of the MT48 gene tagged at the C-terminus with an HA epitope in mt48-/- cells
the mt57-/- mutant cells are complemented with the triple MT57 mutant W62D/G63D/Q64D and with MT57 containing the K266A mutation, both mutants do not reestablish the +5 primer extension stop to wild-type levels
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the shRNA-mediated knockdown of transcription factor Pax6 reveals downregulation of a set of direct target genes, including Cap2, Farp1, Pax6, Plekha1, Prox1, Tshz2, and Zfp536
there are elevated isoform CMTr1 levels during early embryogenesis and a peak of both isoforms CMTr1 and CMTr2 in prepupae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arhin, G.K.; Li, H.; Ullu, E.; Tschudi, C.
A protein related to the vaccinia virus cap-specific methyltransferase VP39 is involved in cap 4 modification in Trypanosoma brucei
RNA
12
53-62
2006
Trypanosoma brucei (Q38DJ3)
brenda
Arhin, G.; Ullu, E.; Tschudi, C.
2'-O-Methylation of position 2 of the trypanosome spliced leader cap 4 is mediated by a 48 kDa protein related to vaccinia virus VP39
Mol. Biochem. Parasitol.
147
137-139
2006
Trypanosoma brucei (Q385S9)
brenda
Werner, M.; Purta, E.; Kaminska, K.; Cymerman, I.; Campbell, D.; Mittra, B.; Zamudio, J.; Sturm, N.; Jaworski, J.; Bujnicki, J.
2'-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family
Nucleic Acids Res.
39
4756-4768
2011
Homo sapiens (Q8IYT2), Homo sapiens
brenda
Smietanski, M.; Werner, M.; Purta, E.; Kaminska, K.; Stepinski, J.; Darzynkiewicz, E.; Nowotny, M.; Bujnicki, J.
Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation
Nat. Commun.
5
3004
2014
Homo sapiens (Q8IYT2), Homo sapiens
brenda
Sun, J.; Zhao, Y.; McGreal, R.; Cohen-Tayar, Y.; Rockowitz, S.; Wilczek, C.; Ashery-Padan, R.; Shechter, D.; Zheng, D.; Cvekl, A.
Pax6 associates with H3K4-specific histone methyltransferases Mll1, Mll2, and Set1a and regulates H3K4 methylation at promoters and enhancers
Epigenetics Chromatin
9
37
2016
Mus musculus (Q9CYT6)
brenda
Haussmann, I.U.; Wu, Y.; Nallasivan, M.P.; Archer, N.; Bodi, Z.; Hebenstreit, D.; Waddell, S.; Fray, R.; Soller, M.
CMTr cap-adjacent 2-O-ribose mRNA methyltransferases are required for reward learning and mRNA localization to synapses
Nat. Commun.
13
1209
2022
Drosophila melanogaster
brenda
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