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Information on EC 2.1.1.230 - 23S rRNA (adenosine1067-2'-O)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.230
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.230 23S rRNA (adenosine1067-2'-O)-methyltransferase
IUBMB Comments
The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
show+
=
+
+
adenosine1067 in 23S rRNA
=
+
2'-O-methyladenosine1067 in 23S rRNA
Synonyms
nosiheptide-resistance methyltransferase, thiostrepton-resistance methyltransferase, nhr protein, nosiheptide resistance methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.1.1.66
-
-
formerly
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (adenosine1067-2'-O)-methyltransferase
The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton [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 + adenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli
S-adenosyl-L-homocysteine + 2'-O-methyladenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
S-adenosyl-L-methionine + adenosine1067 in Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in Escherichia coli 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
Substrates: as 58 nucleotide substrate for methylation, or as shortened 29 nt hairpin substrate, local base-base interactions play an important role in aligning the substrate 2'-hydroxyl group of A1067 for methyl group transfer, stoichiometry of RNA binding by the NHR dimer, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: Streptomyces azureus is the producer of the peptide antibiotic thiostrepton. Thiostrepton inhibits protein synthesis by binding to the complex of 23S rRNA and protein L-11 which blocks processes associated with the GTP-hydrolysis center of the ribosome including the binding of guanine nucleotides, elongation factor proteins and tRNA. 23S rRNA (adenosine1067-2'-O)-methyltransferase confers resistance to tthiostrepton
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: the enzyme is involved in resistance to thiostrepton
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: the methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: RNA sequence variants of the RNA fragment with mutations in nucleotides 1051-1108 are tested as substrates for the methylase. Methylation is dependent on the secondary structure of the hairpin including nucleotide A1067 and the exact sequence U(1066)-A(1067)-G(1068)-A(1O69)-A(1070) of the single strand
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
Substrates: enzyme Tsr uses the co-substrate AdoMet to methylate the 23 S rRNA, presumably prior to the assembly of the 50 S subunit as the L11 and proposed Tsr binding surfaces are overlapping
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
Substrates: 58-nt RNA substrate secondary structure, and key longrange interactions within the 58-nt domain tertiary fold, overview
Products: -
Products: -
?
additional information
?
-
Substrates: compared the methylation activity of the Arg135Ala NHR heterodimer with the wild-type NHR homodimer and a series of 29 nt wild-type and mutant RNA substrates. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer. Construction of diverse mutant RNA substrates in which A1067 is replaced by adenine structural analogues, A1067G retains significant activity, while 7-deaza-A and 1-methyl-A substitutions at A1067 reduce the activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: compared the methylation activity of the Arg135Ala NHR heterodimer with the wild-type NHR homodimer and a series of 29 nt wild-type and mutant RNA substrates. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer. Construction of diverse mutant RNA substrates in which A1067 is replaced by adenine structural analogues, A1067G retains significant activity, while 7-deaza-A and 1-methyl-A substitutions at A1067 reduce the activity, overview
Products: -
Products: -
?
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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 + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: Streptomyces azureus is the producer of the peptide antibiotic thiostrepton. Thiostrepton inhibits protein synthesis by binding to the complex of 23S rRNA and protein L-11 which blocks processes associated with the GTP-hydrolysis center of the ribosome including the binding of guanine nucleotides, elongation factor proteins and tRNA. 23S rRNA (adenosine1067-2'-O)-methyltransferase confers resistance to tthiostrepton
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: the enzyme is involved in resistance to thiostrepton
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
-
Substrates: the methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton
Products: -
Products: -
?
S-adenosyl-L-methionine + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
Substrates: enzyme Tsr uses the co-substrate AdoMet to methylate the 23 S rRNA, presumably prior to the assembly of the 50 S subunit as the L11 and proposed Tsr binding surfaces are overlapping
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Protein L11
-
binding of either thiostrepton or protein L11 inhibits methylation
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S-Adenosyl-D-homocysteine
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competitivewith respect to S-adenosyl-L-methionine
Thiostrepton
-
binding of either thiostrepton or protein L11 inhibits methylation
additional information
stabilizing the RNA tertiary structure, as in RNA mutant U1061A, decreases Tsr binding affinity and catalytic activity independent of RNA structural changes
-
additional information
-
stabilizing the RNA tertiary structure, as in RNA mutant U1061A, decreases Tsr binding affinity and catalytic activity independent of RNA structural changes
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
adenosine in an RNA fragment containing nucleotides 1029-1122 of the 23S ribosomal RNA from Escherichia coli
-
pH 7.5, 35Ā°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.8
-
pH 7.0: about 60% of maximal activity, pH 7.8: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
malfunction
in the absence of the N-terminal domain, Tsr is catalytically inactive despite possessing the intact S-adenosyl-L-methionine binding sites and catalytic center. The Tsr-C-terminal domain dimer binds the RNA 30fold more weakly than the wild-type enzyme and is unable to promote the N-terminal domain-dependent RNA conformational change
physiological function
additional information
physiological function
methylation at adenosine1067 in 23S rRNA is essential for resistance against nosiheptide, a sulfur peptide antibiotic, which is produced by the nosiheptide-producing strain, Streptomyces actuosus
physiological function
-
Streptomyces azureus is the producer of the peptide antibiotic thiostrepton. Thiostrepton inhibits protein synthesis by binding to the complex of 23S rRNA and protein L-11 which blocks processes associated with the GTP-hydrolysis center of the ribosome including the binding of guanine nucleotides, elongation factor proteins and tRNA. 23S rRNA (adenosine1067-2'-O)-methyltransferase confers resistance to thiostrepton
physiological function
-
the enzyme is involved in resistance to thiostrepton
physiological function
-
the methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton
physiological function
the nosiheptide producer Streptomyces actuosis prevents self-intoxication by expressing the enzyme, which methylates the 2'-hydroxyl of 23 S rRNA nucleotide adenosine 1067 within the antibiotic binding site. Methylation at A1067 blocks thiazole binding directly. This region of 23S rRNA is also the binding site for the ribosomal protein L11
physiological function
the thiostrepton producer Streptomyces azureus prevents self-intoxication by expressing the thiostrepton-resistance methyltransferase (Tsr), which methylates the 2'-hydroxyl of 23 S rRNA nucleotide adenosine 1067 within the thiostrepton binding site
additional information
each protomer of the homodimer containing an L30e-like amino-terminal domain and a SPOUT methyltransferase family catalytic carboxyl-terminal domain, both enzyme domains are required for high affinity RNA substrate binding. The Tsr-C-terminal domain has intrinsic, weak RNA affinity that is necessary to direct the specific high-affinity Tsr-RNA interaction via N-terminal domains, which have no detectable RNA affinity when isolated. The N-terminal domains increase RNA binding affinity and are necessary for catalysis, RNA binding mechanism, overview. The N-terminal domain of Tsr is an essential component of the RNA substrate recognition mechanism by both promoting high affinity RNA binding and activation of catalysis by the C-terminal domain
additional information
-
each protomer of the homodimer containing an L30e-like amino-terminal domain and a SPOUT methyltransferase family catalytic carboxyl-terminal domain, both enzyme domains are required for high affinity RNA substrate binding. The Tsr-C-terminal domain has intrinsic, weak RNA affinity that is necessary to direct the specific high-affinity Tsr-RNA interaction via N-terminal domains, which have no detectable RNA affinity when isolated. The N-terminal domains increase RNA binding affinity and are necessary for catalysis, RNA binding mechanism, overview. The N-terminal domain of Tsr is an essential component of the RNA substrate recognition mechanism by both promoting high affinity RNA binding and activation of catalysis by the C-terminal domain
additional information
the NHR heterodimer requires only one functional subunit for RNA recognition and enzymatic activity. The catalytic residue is Arg135
additional information
-
the NHR heterodimer requires only one functional subunit for RNA recognition and enzymatic activity. The catalytic residue is Arg135
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A086BPG7_9BIFI
280
0
30499
TrEMBL
-
Q7UG85_RHOBA
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
281
0
30202
TrEMBL
-
D5UK31_CELFN
Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 / NCIMB 8073 / NRS 134)
264
0
27214
TrEMBL
-
D2QAT2_BIFDB
Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1)
290
0
31306
TrEMBL
-
A0A5K1UNQ6_PLAKH
2247
0
258606
TrEMBL
Secretory Pathway (Reliability: 2)
K4ISW1_BIFAP
Bifidobacterium asteroides (strain PRL2011)
330
0
35088
TrEMBL
-
A0A518BBS2_9BACT
268
0
28737
TrEMBL
-
A0A2N9BJP1_STRCX
269
0
28977
TrEMBL
-
A0A1V5VV30_9BACT
181
0
20254
TrEMBL
-
A0A1J1HD87_PLARL
2169
0
261184
TrEMBL
other Location (Reliability: 1)
A0A644YUX1_9ZZZZ
237
0
26723
TrEMBL
other Location (Reliability: 2)
A0A385ZR55_9ACTN
257
0
26755
TrEMBL
-
A0A1C6XQB3_PLACH
2296
0
271499
TrEMBL
other Location (Reliability: 2)
A0A0Y9X4A3_PLABE
2306
0
274948
TrEMBL
other Location (Reliability: 2)
D2QA44_BIFDB
Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1)
288
0
31890
TrEMBL
-
B7PXR1_IXOSC
229
0
25613
TrEMBL
other Location (Reliability: 3)
C0XQB8_CORLD
Corynebacterium lipophiloflavum (strain ATCC 700352 / DSM 44291 / CCUG 37336 / JCM 10383 / DMMZ 1944)
273
0
29586
TrEMBL
-
K4IQX0_BIFAP
Bifidobacterium asteroides (strain PRL2011)
341
0
36207
TrEMBL
-
A0A518F0R3_9BACT
177
0
19713
TrEMBL
-
A0A1D3LK91_PLACH
2295
0
271463
TrEMBL
other Location (Reliability: 2)
A0A1C6XE89_PLACH
2296
0
271525
TrEMBL
other Location (Reliability: 2)
A0A653HP89_9APIC
1309
5
152017
TrEMBL
Secretory Pathway (Reliability: 5)
C2GIF2_9CORY
276
0
29635
TrEMBL
-
K4IMM6_BIFAP
Bifidobacterium asteroides (strain PRL2011)
317
0
34699
TrEMBL
-
K4ILI2_BIFAP
Bifidobacterium asteroides (strain PRL2011)
288
0
31651
TrEMBL
-
F7XRP6_TREPU
Treponema paraluiscuniculi (strain Cuniculi A)
319
0
35546
TrEMBL
-
B0SMX6_LEPBP
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
277
0
30908
TrEMBL
-
A0A060S506_PLARE
2877
0
345767
TrEMBL
other Location (Reliability: 3)
A0A1V6G7U0_9DELT
248
0
26175
TrEMBL
-
J7KYH7_NOCAA
Nocardiopsis alba (strain ATCC BAA-2165 / BE74)
269
0
29439
TrEMBL
-
Q8NS54_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
276
0
29861
TrEMBL
-
F7XRU9_TREPU
Treponema paraluiscuniculi (strain Cuniculi A)
292
0
31133
TrEMBL
-
A0A094INT0_9BACT
236
0
26616
TrEMBL
-
A0A077YHA4_PLAYE
2379
0
282446
TrEMBL
other Location (Reliability: 2)
A0A1D3LEN8_PLACH
2296
0
271624
TrEMBL
other Location (Reliability: 2)
A0A0H3EEM0_BIFBP
Bifidobacterium bifidum (strain PRL2010)
332
0
35380
TrEMBL
-
TSNR_STRAJ
269
0
28901
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
dimerization is required for methyltransferase activity
homodimer
each protomer containing an L30e-like amino-terminal domain and a SPOUT methyltransferase family catalytic carboxyl-terminal domain, both enzyme domains are required for high affinity RNA substrate binding, Tsr domain organization, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the enzyme and the enzyme in complex with S-adenosyl-L-methionine at 2.0 and 2.1 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H258A/E259A
double mutaion decreases methyltransferase activity to 40% compared to wild-type activity
R135A
R162A
site-directed mutagenesis, the mutant binds RNA with 100fold weaker affinity than wild-type Tsr
R26A
site-directed mutagenesis, the mutant is unable to promote the RNase V1-sensitive RNA structural changes, but maintains its interaction with the RNA under certain conditions for the protection of nucleotides G1068 and G1071 from cleavage by RNase T1
R135A
site-directed mutagenesis, the inactive R135A mutant homodimer binds to the RNA causing a shift in electrophoretic mobility, and the heterodimer composed of active and inactive subunits also binds the RNA efficiently. The inactive heterodimer complex binds the RNA more efficiently than the inactive mutant homodimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity and heparin affinity chromatography, followed by gel filtration
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tsr, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes, with additional FLAG and HA tags, in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thompson, J.; Cundliffe, E.
Purification and properties of an RNA methylase produced by Streptomyces azureus and involved in resistance to thiostrepton
J. Gen. Microbiol.
124
291-297
1981
Streptomyces azureus
-
brenda
Thompson, J.; Schmidt, F.; Cundliffe, E.
Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton
J. Biol. Chem.
257
7915-7917
1982
Streptomyces azureus
brenda
Bechthold, A.; Floss, H.G.
Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2'-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA
Eur. J. Biochem.
224
431-437
1994
Streptomyces azureus
brenda
Yang, H.; Wang, Z.; Shen, Y.; Wang, P.; Jia, X.; Zhao, L.; Zhou, P.; Gong, R.; Li, Z.; Yang, Y.; Chen, D.; Murchie, A.I.; Xu, Y.
Crystal structure of the nosiheptide-resistance methyltransferase of Streptomyces actuosus
Biochemistry
49
6440-6450
2010
Streptomyces actuosus (P52391), Streptomyces actuosus
brenda
Kuiper, E.G.; Conn, G.L.
Binding induced RNA conformational changes control substrate recognition and catalysis by the thiostrepton resistance methyltransferase (Tsr)
J. Biol. Chem.
289
26189-26200
2014
Streptomyces azureus (P18644), Streptomyces azureus
brenda
Yin, S.; Jiang, H.; Chen, D.; Murchie, A.I.
Substrate recognition and modification by the nosiheptide resistance methyltransferase
PLoS ONE
10
e0122972
2015
Streptomyces actuosus (P52391), Streptomyces actuosus
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.230)
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