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Information on EC 2.1.1.297 - peptide chain release factor N5-glutamine methyltransferase
for references in articles please use BRENDA:EC2.1.1.297
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.297 peptide chain release factor N5-glutamine methyltransferase
IUBMB Comments
Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity.
The enzyme appears in viruses and cellular organisms
- 2.1.1.297
- histone
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coactivator
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coactivator-associated
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methyltransferases
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prmts
- dimethylarginine
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h3r2me2a
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sdmas
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picln
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di-methylation
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h4r3me2s
Reaction Schemes
show+
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[peptide chain release factor 1 or 2]-L-glutamine
=
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[peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
Synonyms
hemk2, hemk1, n5-glutamine methyltransferase, prmc/hemk, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HemK
Hemk1
Hemk2
Mtq2
Mtq2-Trm112 methyltransferase
N5-glutamine methyltransferase
N5-glutamine MTase
N5-glutamine S-adenosyl-L-methionine dependent methyltransferase
PrmC
PrmC/HemK
release factor glutamine methyltransferase
TM0488
N5-glutamine S-adenosyl-L-methionine dependent methyltransferase
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N5-glutamine S-adenosyl-L-methionine dependent methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[peptide chain release factor 1 or 2]-L-glutamine (N5-glutamine)-methyltransferase
Modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity.
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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 + [CHD5]-L-glutamine
S-adenosyl-L-homocysteine + [CHD5]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [eukaryotic ribosomal release factor 1]-L-glutamine185
S-adenosyl-L-homocysteine + [eukaryotic ribosomal release factor 1]-N5-methyl-L-glutamine185
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S-adenosyl-L-methionine + [eukaryotic translation termination factor eRF1]-L-glutamine
S-adenosyl-L-homocysteine + [eukaryotic translation termination factor eRF1]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [mitochondrial release factor 1L]-L-glutamine252
S-adenosyl-L-homocysteine + [mitochondrial release factor 1L]-N5-methyl-L-glutamine252
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S-adenosyl-L-methionine + [mitochondrial release factor 1]-L-glutamine313
S-adenosyl-L-homocysteine + [mitochondrial release factor 1]-N5-methyl-L-glutamine313
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S-adenosyl-L-methionine + [mitochondrial release factor MRPL58]-L-glutamine90
S-adenosyl-L-homocysteine + [mitochondrial release factor MRPL58]-N5-methyl-L-glutamine90
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S-adenosyl-L-methionine + [mitochondrial release factor R]-L-glutamine73
S-adenosyl-L-homocysteine + [mitochondrial release factor R]-N5-methyl-L-glutamine73
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S-adenosyl-L-methionine + [NUT]-L-glutamine
S-adenosyl-L-homocysteine + [NUT]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [eukaryotic translation termination factor eRF1]-L-glutamine
S-adenosyl-L-homocysteine + [eukaryotic translation termination factor eRF1]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [eukaryotic translation termination factor eRF1]-L-glutamine
S-adenosyl-L-homocysteine + [eukaryotic translation termination factor eRF1]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
Substrates: -
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additional information
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Substrates: PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: isoform HemK methylates peptide release factors RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and hemK is required for the methylation within the same fragment of, at least, RF1 in vivo
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additional information
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Substrates: no evidence for a DNA adenine-methyltransferase activity
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additional information
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Q6PRU9
Substrates: no evidence for a DNA adenine-methyltransferase activity
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additional information
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Substrates: the enzyme prefers methylation of G-Q-X3-R motifs. The enzyme also has a lysine methyltransferase activity on lysine 12 of histone H4 (H4K12) as well as on peptides CNIPF, EI2BD, ICEF1, MN213, TSN19, UBR4, UXS1, and KCAB2. The enzyme prefers methylation of Q over K as methylation target at peptide and protein level and additionally the eukaryotic ribosomal release factor 1 sequence context is preferred over the H4K12 sequence
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Substrates: the catalytic methyl transfer by methyltransferase HemK is an energy-favored process with an activation barrier of 15.7 kcal/mol and an exothermicity of 12.0 kcal/mol, while the coenzyme-modified HemK is unable to catalyze the methyl transfer because of a substantial barrier of 20.6 kcal/mol and instability of the product intermediate. Therefore the nitrogen analogue of the SAM coenzyme should be a practicable inhibitor for the catalytic methyl transfer by HemK. The protein environment, especially the residues Asn197 and Pro198 in the active site, plays a pivotal role in stabilizing the transition state and regulating the positioning of reactive groups
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additional information
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Substrates: the catalytic methyl transfer by methyltransferase HemK is an energy-favored process with an activation barrier of 15.7 kcal/mol and an exothermicity of 12.0 kcal/mol, while the coenzyme-modified HemK is unable to catalyze the methyl transfer because of a substantial barrier of 20.6 kcal/mol and instability of the product intermediate. Therefore the nitrogen analogue of the SAM coenzyme should be a practicable inhibitor for the catalytic methyl transfer by HemK. The protein environment, especially the residues Asn197 and Pro198 in the active site, plays a pivotal role in stabilizing the transition state and regulating the positioning of reactive groups
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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 + [eukaryotic translation termination factor eRF1]-L-glutamine
S-adenosyl-L-homocysteine + [eukaryotic translation termination factor eRF1]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
S-adenosyl-L-methionine + [eukaryotic translation termination factor eRF1]-L-glutamine
S-adenosyl-L-homocysteine + [eukaryotic translation termination factor eRF1]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [eukaryotic translation termination factor eRF1]-L-glutamine
S-adenosyl-L-homocysteine + [eukaryotic translation termination factor eRF1]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
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S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 1]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 1]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
Substrates: -
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S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
Substrates: -
Products: -
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S-adenosyl-L-methionine + [peptide chain release factor 2]-L-glutamine
S-adenosyl-L-homocysteine + [peptide chain release factor 2]-N5-methyl-L-glutamine
Substrates: -
Products: -
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additional information
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Substrates: PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: PrmC methylates chlamydia peptide release factors within the tryptic fragment containing the universally conserved sequence motif Gly-Gly-Gln
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additional information
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Substrates: isoform HemK methylates peptide release factors RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and hemK is required for the methylation within the same fragment of, at least, RF1 in vivo
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TRMT112
the enzyme requires the interaction partner TRMT112 for complete methyltransferase activity and stability
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
stopped-flow kinetics, linear kinetic model
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
Q6SKR2, Q6PRU9
abundant mRNA expression in embryonic stem cells, weak expression in differentiated embryonic stem cells, protein is most abundant in undifferentiated embryonic stem cells
brenda
Q6SKR2, Q6PRU9
abundant mRNA expression in embryonic stem cells, weak expression in differentiated embryonic stem cells, proein is most abundant in undifferentiated embryonic stem cells
brenda
additional information
no expression in muscle, heart, placenta, pancreas, lung and stomach
brenda
additional information
Q6PRU9
no expression in muscle, heart, placenta, pancreas, lung and stomach
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q6SKR2, Q6PRU9
isoform HemK1 is detected mainly in the nucleus of COS7 cell lines after 24 h post-transfection
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
enzyme deletion leads to severe growth impairment in yeast
malfunction
disruption of the HEMK1 gene has no considerable impact on the overall cell growth, mitochondrial DNA copy number, mitochondrial membrane potential, and mitochondrial protein synthesis under regular culture condition with glucose as a carbon source
malfunction
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enzyme deletion leads to severe growth impairment in yeast
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physiological function
the enzyme modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity
physiological function
deletion of peptide release factor N5-glutamine methylase leads to very poor growth on rich media and abolishes methylation of release factor RF1. Fast growing spontaneous revertants of the deletion strain contain the mutation T246A or T246S in release factor RF2
physiological function
chlamydial isoform PrmC expression suppresses the growth defect of a prmC knockout strain of Escherichia coli K-12. Overexpression of PrmC in Escherichia coli strongly retards growth to the level of neative control
physiological function
a hemK knockout suffers severe growth defects and shows a global shift in gene expression to anaerobic respiration. This shift may lead to the abrogation of photosensitivity by reducing the oxidative stress. Suppressor mutations that abrogate the growth defects of the hemK knockout strain are caused by a threonine to alanine change at codon 246 of polypeptide chain release factor RF2, indicating that hemK plays a role in translational termination. The hemK knockout strain shows an enhanced rate of read-through of nonsense codons and induction of transfer-mRNA-mediated tagging of proteins within the cell. HemK methylates RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and hemK is required for the methylation within the same fragment of, at least, RF1 in vivo
physiological function
the methylation activity of the enzyme Mtq2 is important for cell growth and antibiotic resistance. Mtq2 is a ribosome assembly factor important for large ribosomal subunit formation. Mtq2 is associated with nuclear 60S subunit precursors, and its catalytic activity is required for nucleolar release of pre-60S and for efficient production of mature 5.8S and 25S rRNAs. Mtq2-Trm112 may modify eukaryotic translation termination factor eRF1 in the nucleus as part of a quality control mechanism aimed at proof-reading the peptidyl transferase center, where it will subsequently bind during translation termination
physiological function
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the methylation activity of the enzyme Mtq2 is important for cell growth and antibiotic resistance. Mtq2 is a ribosome assembly factor important for large ribosomal subunit formation. Mtq2 is associated with nuclear 60S subunit precursors, and its catalytic activity is required for nucleolar release of pre-60S and for efficient production of mature 5.8S and 25S rRNAs. Mtq2-Trm112 may modify eukaryotic translation termination factor eRF1 in the nucleus as part of a quality control mechanism aimed at proof-reading the peptidyl transferase center, where it will subsequently bind during translation termination
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physiological function
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the enzyme modifies the glutamine residue in the universally conserved glycylglycylglutamine (GGQ) motif of peptide chain release factor, resulting in almost complete loss of release activity
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physiological function
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chlamydial isoform PrmC expression suppresses the growth defect of a prmC knockout strain of Escherichia coli K-12. Overexpression of PrmC in Escherichia coli strongly retards growth to the level of neative control
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additional information
analysis of folding of a small five-helix protein domain at the N-terminal domain of Escherichia coli N5-glutamine methyltransferase HemK in real time. The isolated HemK N-terminal domain (residues 1 to 73) forms a stable alpha-helical structure independent of the C-terminal domain. Cotranslational folding of the protein, which folds autonomously and rapidly in solution, proceeds through a compact, non-native conformation that forms within the peptide tunnel of the ribosome. The compact state rearranges into a native-like structure immediately after the full domain sequence has emerged from the ribosome. Both folding transitions are rate-limited by translation, allowing for quasi-equilibrium sampling of the conformational space restricted by the ribosome. Cotranslational folding may be typical of small, intrinsically rapidly folding protein domains
additional information
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analysis of folding of a small five-helix protein domain at the N-terminal domain of Escherichia coli N5-glutamine methyltransferase HemK in real time. The isolated HemK N-terminal domain (residues 1 to 73) forms a stable alpha-helical structure independent of the C-terminal domain. Cotranslational folding of the protein, which folds autonomously and rapidly in solution, proceeds through a compact, non-native conformation that forms within the peptide tunnel of the ribosome. The compact state rearranges into a native-like structure immediately after the full domain sequence has emerged from the ribosome. Both folding transitions are rate-limited by translation, allowing for quasi-equilibrium sampling of the conformational space restricted by the ribosome. Cotranslational folding may be typical of small, intrinsically rapidly folding protein domains
additional information
the N-terminal alpha-helical domain of the universally conserved N5-glutamine methyltransferase HemK is compacted within the exit tunnel and rearranges into the native fold upon emerging from the ribosome. Analysis of the rapid kinetics of translation and folding monitored by fluorescence resonance energy transfer and photoinduced electron transfer using global fitting to a model for synthesis of the 112-amino acid HemK fragment. The co-translational folding trajectory of HemK starts within the tunnel and passes through four kinetically distinct folding intermediates that may represent sequential docking of helices to a growing compact core. The kinetics of the process is defined entirely by translation
additional information
the cotranslational folding of two small protein domains of different folds - the alpha-helical N-terminal domain of HemK and the beta-rich FLN5 filamin domain - by measuring the force that the folding protein exerts on the nascent chain when located in different parts of the ribosome exit tunnel (force-profile analysis, or FPA), allowing us to compare FPA to three other techniques currently used to study cotranslational folding: real-time FRET, photoinduced electron transfer, and NMR, method evaluation, overview
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structure of the HemK N-terminal domain, PDB ID 1T43
molecular replacement based on the data of Thermotoga maritima enzyme, in complex with the methyl-donor product S-adenosyl-L-homocysteine. Enzyme HemK contains two domains: a putative substrate binding domain at the N-terminus consisting of a five helix bundle and a seven-stranded catalytic domain at the C-terminus that harbors the binding site for S-adenosyl-L-homocysteine. The two domains are linked by a beta-hairpin. The apparent hinge mobility of the two domains may reflect functional importance during the reaction cycle
crystallized in the presence of S-adenosylmethionine at 223°C using ammonium sulfate as the precipitant. X-ray diffraction data are collected to 2.5 A resolution from a native crystal. The crystal is orthorhombic, belonging to the space group I222 (or I2(1)2(1)2(1)), with unit-cell parameters of a = 104.24, b = 118.73, and c = 146.62 A. Two (or three) monomers of recombinant HemK are likely to be present in the crystallographic asymmetric unit
to 2.2 A resolution. The C-terminal domain of PrmC adopts the canonical S-adenosyl-L-methionine-dependent methyltransferase fold and shares structural similarity with the nucleotide N-methyltransferases in the active site, including use of a conserved (D/N)PPY motif to select and position the glutamine substrate. Residues of the PrmC 197NPPY200 motif form hydrogen bonds that position the planar Gln side chain such that the lone-pair electrons on the nitrogen nucleophile are oriented toward the methyl group of S-adenosyl-Lmethionine. In the product complex, the methyl group remains pointing toward the sulfur, consistent with either an sp3-hybridized, positively charged Gln nitrogen, or a neutral sp2-hybridized nitrogen in a strained conformation. Due to steric overlap within the active site, proton loss and formation of the neutral planar methylamide product are likely to occur during or after product release
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L28A
site-directed mutagenesis, the L28A mutation reduces the in vitro denaturation temperature of HemK-N-terminal domain from 50°C to 30°C
D77A
the catalytic mutant is largely unable to methylate eRF1 in vivo
N122A
the catalytic mutant is largely unable to methylate eRF1 in vivo
D77A
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the catalytic mutant is largely unable to methylate eRF1 in vivo
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N122A
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the catalytic mutant is largely unable to methylate eRF1 in vivo
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additional information
additional information
mutated HemK N-terminal domain in which four conserved Leu residues occur, comprising the hydrophobic core of the N-terminal domain, are simultaneously replaced with Ala (4×A)
additional information
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mutated HemK N-terminal domain in which four conserved Leu residues occur, comprising the hydrophobic core of the N-terminal domain, are simultaneously replaced with Ala (4×A)
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
the isolated N-terminal domain with even a single Ala mutation is almost completely unfolded at 37°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography and Ni-NTA agarose bead chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene HEMK1, recombinant expression of isolated N-terminal domain and of truncated mutants in Escherichia coli, cotranslational folding of the HemK N-terminal domain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heurgue-Hamard, V.; Champ, S.; Engstrom, A.; Ehrenberg, M.; Buckingham, R.H.
The hemK gene in Escherichia coli encodes the N5-glutamine methyltransferase that modifies peptide release factors
EMBO J.
21
769-778
2002
Escherichia coli (P0ACC1)
brenda
Yoon, H.J.; Kang, K.Y.; Ahn, H.J.; Shim, S.M.; Ha, J.Y.; Lee, S.K.; Mikami, B.; Suh, S.W.
X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase
Mol. Cells
16
266-269
2003
Thermotoga maritima (Q9WYV8), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WYV8)
brenda
Schubert, H.L.; Phillips, J.D.; Hill, C.P.
Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase
Biochemistry
42
5592-5599
2003
Thermotoga maritima (Q9WYV8), Thermotoga maritima DSM 3109 (Q9WYV8)
brenda
Pannekoek, Y.; Heurgue-Hamard, V.; Langerak, A.A.; Speijer, D.; Buckingham, R.H.; van der Ende, A.
The N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase PrmC/HemK in Chlamydia trachomatis methylates class 1 release factors
J. Bacteriol.
187
507-511
2005
Chlamydia trachomatis (B0B9D1), Chlamydia trachomatis, Chlamydia trachomatis ATCC VR-902B (B0B9D1)
brenda
Wu, R.; Cao, Z.
QM/MM study of catalytic methyl transfer by the N5-glutamine SAM-dependent methyltransferase and its inhibition by the nitrogen analogue of coenzyme
J. Comput. Chem.
29
350-357
2008
Thermotoga maritima (Q9WYV8), Thermotoga maritima DSM 3109 (Q9WYV8)
brenda
Yang, Z.; Shipman, L.; Zhang, M.; Anton, B.P.; Roberts, R.J.; Cheng, X.
Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase
J. Mol. Biol.
340
695-706
2004
Escherichia coli (P0ACC1)
brenda
Nie, D.S.; Liu, Y.B.; Lu, G.X.
Cloning and primarily function study of two novel putative N5-glutamine methyltransferase (Hemk) splice variants from mouse stem cells
Mol. Biol. Rep.
36
2221-2228
2009
Mus musculus (Q6SKR2), Mus musculus (Q6PRU9)
brenda
Nakahigashi, K.; Kubo, N.; Narita, S.; Shimaoka, T.; Goto, S.; Oshima, T.; Mori, H.; Maeda, M.; Wada, C.; Inokuchi, H.
HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination
Proc. Natl. Acad. Sci. USA
99
1473-1478
2002
Escherichia coli (P0ACC1)
brenda
Holtkamp, W.; Kokic, G.; Jaeger, M.; Mittelstaet, J.; Komar, A.A.; Rodnina, M.V.
Cotranslational protein folding on the ribosome monitored in real time
Science
350
1104-1107
2015
Escherichia coli (P0ACC1), Escherichia coli
brenda
Mercier, E.; Rodnina, M.
Co-translational folding trajectory of the HemK helical domain
Biochemistry
57
3460-3464
2018
Homo sapiens (Q9Y5R4)
brenda
Kemp, G.; Kudva, R.; de la Rosa, A.; von Heijne, G.
Force-profile analysis of the cotranslational folding of HemK and filamin domains comparison of biochemical and biophysical folding assays
J. Mol. Biol.
431
1308-1314
2019
Homo sapiens (Q9Y5R4)
-
brenda
Lacoux, C.; Wacheul, L.; Saraf, K.; Pythoud, N.; Huvelle, E.; Figaro, S.; Graille, M.; Carapito, C.; Lafontaine, D.L.J.; Heurgue-Hamard, V.
The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis
Nucleic Acids Res.
48
12310-12325
2020
Saccharomyces cerevisiae (Q03920), Saccharomyces cerevisiae BY4741 (Q03920)
brenda
Weirich, S.; Ulu, G.T.; Chandrasekaran, T.T.; Kehl, J.; Schmid, J.; Dorscht, F.; Kublanovsky, M.; Levy, D.; Jeltsch, A.
Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues
Protein Sci.
33
e4897
2024
Mus musculus (Q6SKR2)
brenda
Fang, Q.; Kimura, Y.; Shimazu, T.; Suzuki, T.; Yamada, A.; Dohmae, N.; Iwasaki, S.; Shinkai, Y.
Mammalian HEMK1 methylates glutamine residue of the GGQ motif of mitochondrial release factors
Sci. Rep.
12
4104
2022
Homo sapiens (Q9Y5R4)
brenda
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