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Literature summary extracted from

  • Sharma, S.; Hartmann, J.; Watzinger, P.; Klepper, A.; Peifer, C.; Koetter, P.; Lafontaine, D.; Entian, K.
    A single N1-methyladenosine on the large ribosomal subunit rRNA impacts locally its structure and the translation of key metabolic enzymes (2018), Sci. Rep., 8, 11904 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.B128 gene rrp8, sequence comparisons and phylogenetic analysis, quantitative enzyme expression analysis, recombinant expression in Saccharomyces cereviaie Rrp8 deficient mutant strain without complementation by the human Rrp8 enzyme Homo sapiens
2.1.1.287 gene rrp8, sequence comparisons and phylogenetic analysis, quantitative enzyme expression analysis Saccharomyces cerevisiae
2.1.1.287 gene rrp8, sequence comparisons and phylogenetic analysis, quantitative enzyme expression analysis, recombinant expression in and complementation of Saccharomyces cereviaie Rrp8 deficient mutant strain Candida albicans
2.1.1.287 gene rrp8, sequence comparisons and phylogenetic analysis, quantitative enzyme expression analysis, recombinant expression in Saccharomyces cereviaie Rrp8 deficient mutant strain without complementation by the Schizosaccharomyces pombe Rrp8 enzyme Schizosaccharomyces pombe

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.B128 additional information siRNA-mediated depletion of NML in HCT-116 cells, impact of an NML knockdown on m1A1322 methylation in HCT-116 cells Homo sapiens
2.1.1.287 G290R rrp8G209R loss of methylation mutant, catalytically dead mutant, the loss of m1A645 leads to structural changes in and around the helix 25.1 region of the 25S rRNA, phenotypes, detailed overview Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.B128 nucleolus NML is primarily localized in the nucleolus Homo sapiens 5730
-
2.1.1.B128 nucleus
-
 Homo sapiens 5634
-
2.1.1.287 nucleus
-
 Saccharomyces cerevisiae 5634
-
2.1.1.287 nucleus
-
 Candida albicans 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.B128 additional information Homo sapiens 25S/28S rRNA of Homo sapiens contains a single m1A methylation in the helix 25.1. Human enzyme NML is able to methylate yeast 25S rRNA in vivo, cf. Ec 2.1.1.287 ?
-
 ?
2.1.1.B128 S-adenosyl-L-methionine + adenine1322 in 28S rRNA Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methyladenine1322 in 28S rRNA
-
 ?
2.1.1.287 additional information Candida albicans 25S/28S rRNA of Candida albicans contains a single m1A methylation in the helix 25.1 ?
-
 ?
2.1.1.287 additional information Schizosaccharomyces pombe 25S/28S rRNA of Schizosaccharomyces pombe contains a single m1A methylation in the helix 25.1 ?
-
 ?
2.1.1.287 additional information Schizosaccharomyces pombe 972 25S/28S rRNA of Schizosaccharomyces pombe contains a single m1A methylation in the helix 25.1 ?
-
 ?
2.1.1.287 additional information Schizosaccharomyces pombe ATCC 24843 25S/28S rRNA of Schizosaccharomyces pombe contains a single m1A methylation in the helix 25.1 ?
-
 ?
2.1.1.287 additional information Candida albicans RM1000 25S/28S rRNA of Candida albicans contains a single m1A methylation in the helix 25.1 ?
-
 ?
2.1.1.287 additional information Candida albicans CBS 356 25S/28S rRNA of Candida albicans contains a single m1A methylation in the helix 25.1 ?
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine643 in 25S rRNA Candida albicans
-
 S-adenosyl-L-homocysteine + N1-methyladenine643 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine643 in 25S rRNA Candida albicans RM1000
-
 S-adenosyl-L-homocysteine + N1-methyladenine643 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine643 in 25S rRNA Candida albicans CBS 356
-
 S-adenosyl-L-homocysteine + N1-methyladenine643 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine645 in 25S rRNA Saccharomyces cerevisiae
-
 S-adenosyl-L-homocysteine + N1-methyladenine645 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine645 in 25S rRNA Saccharomyces cerevisiae ATCC 204508
-
 S-adenosyl-L-homocysteine + N1-methyladenine645 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine670 in 25S rRNA Schizosaccharomyces pombe
-
 S-adenosyl-L-homocysteine + N1-methyladenine670 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine670 in 25S rRNA Schizosaccharomyces pombe 972
-
 S-adenosyl-L-homocysteine + N1-methyladenine670 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine670 in 25S rRNA Schizosaccharomyces pombe ATCC 24843
-
 S-adenosyl-L-homocysteine + N1-methyladenine670 in 25S rRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.B128 Homo sapiens O43159
-
-
2.1.1.287 Candida albicans
-
-
-
2.1.1.287 Candida albicans CBS 356
-
-
-
2.1.1.287 Candida albicans RM1000
-
-
-
2.1.1.287 Saccharomyces cerevisiae P38961
-
-
2.1.1.287 Saccharomyces cerevisiae ATCC 204508 P38961
-
-
2.1.1.287 Schizosaccharomyces pombe Q10257
-
-
2.1.1.287 Schizosaccharomyces pombe 972 Q10257
-
-
2.1.1.287 Schizosaccharomyces pombe ATCC 24843 Q10257
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.B128 HCT-116 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.B128 additional information 25S/28S rRNA of Homo sapiens contains a single m1A methylation in the helix 25.1. Human enzyme NML is able to methylate yeast 25S rRNA in vivo, cf. Ec 2.1.1.287 Homo sapiens ?
-
 ?
2.1.1.B128 S-adenosyl-L-methionine + adenine1322 in 28S rRNA
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methyladenine1322 in 28S rRNA
-
 ?
2.1.1.287 additional information 25S/28S rRNA of Candida albicans contains a single m1A methylation in the helix 25.1 Candida albicans ?
-
 ?
2.1.1.287 additional information 25S/28S rRNA of Schizosaccharomyces pombe contains a single m1A methylation in the helix 25.1 Schizosaccharomyces pombe ?
-
 ?
2.1.1.287 additional information 25S/28S rRNA of Schizosaccharomyces pombe contains a single m1A methylation in the helix 25.1 Schizosaccharomyces pombe 972 ?
-
 ?
2.1.1.287 additional information 25S/28S rRNA of Schizosaccharomyces pombe contains a single m1A methylation in the helix 25.1 Schizosaccharomyces pombe ATCC 24843 ?
-
 ?
2.1.1.287 additional information 25S/28S rRNA of Candida albicans contains a single m1A methylation in the helix 25.1 Candida albicans RM1000 ?
-
 ?
2.1.1.287 additional information 25S/28S rRNA of Candida albicans contains a single m1A methylation in the helix 25.1 Candida albicans CBS 356 ?
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine643 in 25S rRNA
-
 Candida albicans S-adenosyl-L-homocysteine + N1-methyladenine643 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine643 in 25S rRNA
-
 Candida albicans RM1000 S-adenosyl-L-homocysteine + N1-methyladenine643 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine643 in 25S rRNA
-
 Candida albicans CBS 356 S-adenosyl-L-homocysteine + N1-methyladenine643 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine645 in 25S rRNA
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N1-methyladenine645 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine645 in 25S rRNA
-
 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + N1-methyladenine645 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine670 in 25S rRNA
-
 Schizosaccharomyces pombe S-adenosyl-L-homocysteine + N1-methyladenine670 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine670 in 25S rRNA
-
 Schizosaccharomyces pombe 972 S-adenosyl-L-homocysteine + N1-methyladenine670 in 25S rRNA
-
 ?
2.1.1.287 S-adenosyl-L-methionine + adenine670 in 25S rRNA
-
 Schizosaccharomyces pombe ATCC 24843 S-adenosyl-L-homocysteine + N1-methyladenine670 in 25S rRNA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.B128 m1A large subunit rRNA methyltransferase
-
 Homo sapiens
2.1.1.B128 additional information cf. EC 2.1.1.287 Homo sapiens
2.1.1.B128 NML
-
 Homo sapiens
2.1.1.B128 nucleomethylin
-
 Homo sapiens
2.1.1.B128 ribosomal RNA-processing protein 8 UniProt Homo sapiens
2.1.1.B128 Rrp8
-
 Homo sapiens
2.1.1.287 5S rRNA (adenine(645)-N(1))-methyltransferase UniProt Saccharomyces cerevisiae
2.1.1.287 CaRRP8
-
 Candida albicans
2.1.1.287 ribosomal RNA-processing protein 8 UniProt Saccharomyces cerevisiae
2.1.1.287 ribosomal RNA-processing protein 8 UniProt Candida albicans
2.1.1.287 ribosomal RNA-processing protein 8 UniProt Schizosaccharomyces pombe
2.1.1.287 Rrp8
-
 Saccharomyces cerevisiae
2.1.1.287 Rrp8
-
 Candida albicans
2.1.1.287 Rrp8
-
 Schizosaccharomyces pombe

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.B128 S-adenosyl-L-methionine
-
 Homo sapiens
2.1.1.287 S-adenosyl-L-methionine
-
 Saccharomyces cerevisiae
2.1.1.287 S-adenosyl-L-methionine
-
 Candida albicans
2.1.1.287 S-adenosyl-L-methionine
-
 Schizosaccharomyces pombe

General Information

EC Number General Information Comment Organism
2.1.1.B128 evolution the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved Homo sapiens
2.1.1.B128 malfunction siRNA-mediated depletion of NML is highly efficient at mRNA level, impact of an NML knockdown on m1A1322 methylation in HCT-116 cells. Depletion of NML leads to abnormal and altered nucleolar morphology Homo sapiens
2.1.1.B128 physiological function the human nucleomethylin (NML or RRP8) fails to complement the pre-rRNA processing phenotype and the growth cold sensitivity of Saccharomyces cerevisiae DELTArrp8 mutant strain Homo sapiens
2.1.1.287 evolution the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved Saccharomyces cerevisiae
2.1.1.287 evolution the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved Candida albicans
2.1.1.287 evolution the N1-methyladenosine in helix 25.1 of 25/28S rRNA seems to be highly conserved Schizosaccharomyces pombe
2.1.1.287 malfunction Loss of m1A645 in yeast alters the rRNA topology by affecting eL32 interaction with 25S rRNA. Methylation of the N1 atom of adenosine leads to a net positive charge on the base and is expected to disrupt the canonical Watson-Crick base pairing. The loss of m1A645 leads to structural changes in and around the helix 25.1 region of the 25S rRNA and causes formation of stalled preinitiation complex called halfmers. Loss of m1A645 does not influence the conformation of helix 7 and 60S synthesis. But 60S lacking m1A645 are less competent to bind to 40S subunits and therefore cause the formation of halfmers in the absence of m1A645. Loss of m1A645 in yeast alters the rRNA topology by affecting eL32 interaction with 25S rRNA. Loss of Rrp8 leads to an accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth. Both of these phenotypes are fully complemented by Candida albicans CaRRP8, whereas the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity. The human nucleomethylin (NML or RRP8) fails to complement the pre-rRNA processing phenotype and the growth cold sensitivity of DELTArrp8 Saccharomyces cerevisiae
2.1.1.287 physiological function the enzyme CaRRP8 from Candida albicans can fully complement the Saccharomyces cerevisiae rrp8 deficient mutant phenotype, i.e. accumulation of the aberrant 21S pre-rRNA due to defects in A2 cleavage and to cold sensitivity for growth Candida albicans
2.1.1.287 physiological function the expression of Schizosaccharomyces pombe SpRRP8 cannot restore 21S accumulation defects and cold sensitivity in of Saccharomyces cerevisiae DELTArrp8 mutant strain Schizosaccharomyces pombe