Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.183 extracted from

  • Pulicherla, N.; Pogorzala, L.A.; Xu, Z.; O'Farrell, H.C.; Musayev, F.N.; Scarsdale, J.N.; Sia, E.A.; Culver, G.M.; Rife, J.P.
    Structural and functional divergence within the Dim1/KsgA family of rRNA methyltransferases (2009), J. Mol. Biol., 391, 884-893.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E85A 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 Saccharomyces cerevisiae
additional information 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 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
processome Dim1 in eukaryotic organisms is an essential member of the processome, a multifactor assembly that does not exist in bacteria Saccharomyces cerevisiae
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA Saccharomyces cerevisiae 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 4 S-adenosyl-L-homocysteine + N6-dimethyladenosine1779/N6-dimethyladenosine1780 in 18S rRNA
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae C7GSG6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 S-adenosyl-L-methionine + adenine1779/1780 in 18S rRNA
-
Saccharomyces cerevisiae 4 S-adenosyl-L-homocysteine + N6-dimethyladenine1779/N6-dimethyladenine1780 in 18S rRNA
-
?
4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA 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 Saccharomyces cerevisiae 4 S-adenosyl-L-homocysteine + N6-dimethyladenosine1779/N6-dimethyladenosine1780 in 18S rRNA
-
?

Synonyms

Synonyms Comment Organism
ScDim1
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction 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 Saccharomyces cerevisiae