Information on EC 2.1.1.183 - 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.183
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RECOMMENDED NAME
GeneOntology No.
18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA = 4 S-adenosyl-L-homocysteine + N6-dimethyladenine1779/N6-dimethyladenine1780 in 18S rRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase
DIM1 is involved in pre-rRNA processing [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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DIM1 is involved in pre-rRNA processing
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4 S-adenosyl-L-methionine + adenine1779/1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1779/N6-dimethyladenine1780 in 18S rRNA
show the reaction diagram
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?
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1779/N6-dimethyladenine1780 in 18S rRNA
show the reaction diagram
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenosine1779/N6-dimethyladenine1780 in 18S rRNA
show the reaction diagram
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isolation of mutations that uncouple the enzymatic function of Dim1p in methylation from its involvement in prerRNA processing
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?
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenosine1779/N6-dimethyladenosine1780 in 18S rRNA
show the reaction diagram
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neither the bacterial nor the archaeal ortholog could complement for the eukaryotic Dim1. This might be related to the secondary, non-methyltransferase function that Dim1 is known to play in eukaryotic ribosomal maturation
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?
additional information
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the enzyme catalyzed methylation of Escherichia coli 30S ribosomes. The enzyme produces a mixture of N6-methyladenine and 6-dimethyladenine (1.4 times as much N6-methyladenine as N6-dimethyladenine). 80% of the potential sites are methylated after 2 h. Under the assay conditions, ScDim1 releases the N6-methyladenine intermediate, which is subsequently converted to the N6-dimethyladenine product after an additional binding event
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1779/N6-dimethyladenine1780 in 18S rRNA
show the reaction diagram
C7GSG6
Dim1p is required for pre-ribosomal RNA processing
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?
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenosine1779/N6-dimethyladenine1780 in 18S rRNA
show the reaction diagram
-
isolation of mutations that uncouple the enzymatic function of Dim1p in methylation from its involvement in prerRNA processing
-
-
?
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenosine1779/N6-dimethyladenosine1780 in 18S rRNA
show the reaction diagram
-
neither the bacterial nor the archaeal ortholog could complement for the eukaryotic Dim1. This might be related to the secondary, non-methyltransferase function that Dim1 is known to play in eukaryotic ribosomal maturation
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-
?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Dim1 in eukaryotic organisms is an essential member of the processome, a multifactor assembly that does not exist in bacteria
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Dim1 complements heterologously for ksgA- mutation in Escherichia coli, demonstrating functional equivalence of the two proteins
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to delineate regions of the eukaryotic Dim1 critical to its function, KsgA/Dim1 chimeras are created and tested. Construction of six chimeras that result from swapping the two domains of Saccharomyces cerevisiae Dim1, Escherichia coli KsgA, and Methanocaldococcus jannaschii Dim1. Of the chimeras, only one constructed with the N-terminal domain from eukaryotic Dim1 and the C-terminal domain from archaeal Dim1 is able to complement for the eukaryotic Dim1
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E85A
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the altered protein is able to complement for Dim1 but yields a protein with no catalytic activity as determined by primer extension of 18S rRNA. The expected primer extension stops at 1779 and 1780 are missing in rRNA extracted from the strain expressing catalytically inactive ScDim1. The single mutant shows no change in growth rate of yeast at 18, 25, 30, and 37°C
additional information
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to delineate regions of the eukaryotic Dim1 critical to its function, KsgA/Dim1 chimeras are created and tested. Construction of six chimeras that result from swapping the two domains of Saccharomyces cerevisiae Dim1, Escherichia coli KsgA, and Methanocaldococcus jannaschii Dim1. Of the chimeras, only one constructed with the N-terminal domain from eukaryotic Dim1 and the C-terminal domain from archaeal Dim1 is able to complement for the eukaryotic Dim1, suggesting that eukaryotic-specific Dim1 function resides in the N-terminal domain, where few structural differences are observed between members of the KsgA/Dim1 family