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S-adenosyl-L-methionine + m7G-(5')pppGpApApA
?
-
-
-
?
S-adenosyl-L-methionine + ApppGR-RNA
?
S-adenosyl-L-methionine + brome mosaic virus RNA
?
-
-
-
-
r
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
S-adenosyl-L-methionine + m7GpppGp
S-adenosyl-L-homocysteine + m7GpppGmp
-
substrate of minimal chain length for the cap-specific enzyme, m7GpppG is no substrate
-
-
?
S-adenosyl-L-methionine + m7GpppGpN
S-adenosyl-L-homocysteine + m7GpppGmpN
-
-
-
-
?
S-adenosyl-L-methionine + m7GpppGpNp
?
-
-
-
-
?
S-adenosyl-L-methionine + m7GpppGpUbiotin-p
?
-
-
-
-
?
S-adenosyl-L-methionine + RNA chain length 2-6 nt
?
-
-
-
-
r
S-adenosyl-L-methionine + RNA chain length 20-50 nt
?
-
-
-
-
r
additional information
?
-
S-adenosyl-L-methionine + ApppGR-RNA
?
-
adenine-capped RNA, wild-type and mutants, indicating the redundancy of m7G-contact residues able to confer cap-type specificity
-
-
?
S-adenosyl-L-methionine + ApppGR-RNA
?
-
synthetic substrate with unusual cap structure, 20% activity compared to m7G-terminated substrates
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
adenine-capped RNA, wild-type and mutants, indicating the redundancy of m7G-contact residues able to confer cap-type specificity
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
poor substrates are m7GpppN-dinucleotides
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
much less active with poly(G), poly(U) and poly(C)
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
unmethylated vaccinia virus mRNA
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
methylates 2'-O-position of penultimate nucleoside of RNA, no methylation of internal sites
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
methylates 2'-O-position of penultimate nucleoside of RNA, no methylation of internal sites
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
best substrates are poly(A)-nucleosides and poly-(I)-nucleosides with m7G(5')pppN-ends
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
specific, in vitro methyl group acceptors are polyribonucleosides containing 7-methylguanine(5')pppG-terminals
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
specific, in vitro methyl group acceptors are polyribonucleosides containing 7-methylguanine(5')pppG-terminals
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
brome mosaic virus RNA ending in m7G(5')pppG as substrate
mRNA containing a 2'-O-methylpurine cap, R may be guanine or adenosine, prereplicative viral product
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
RNA-polymerase holoenzyme has methyltransferase activity: the same protein acts as methyltransferase and poly(A)-polymerase stimulatory factor VP39
-
-
?
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
-
final step in formation of 7-methylguanosine(5')pppNm-cap structure of viral RNA
-
-
?
additional information
?
-
-
no substrates are RNAs with pN-, ppN-, guanine(5')pppN-terminals
-
-
?
additional information
?
-
-
poly(A) and internal nucleotides of RNA
-
-
?
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5',N8-Adenosyl-alpha,beta-diaminobutyric acid
-
moderate
7-methylguanosine(5')pppN-dinucleotides
-
weak, competitive
S-(2-azaadenosyl)-L-homocysteine
-
-
S-(3'-aminoadenosyl)-L-homocysteine
-
-
S-(3-deazaadenosyl)-L-homocysteine
-
strong
S-(8-azaadenosyl)-L-homocysteine
-
weak
S-(N6-Dimethyl-3-deazaadenosyl)-L-homocysteine
-
weak
S-(N6-Methyladenosyl)-L-homocysteine
-
-
S-Adenosyl-D-homocysteine
-
-
S-adenosyl-L-cysteine
-
moderate
S-adenosyl-L-homocysteine
S-Adenosyl-L-homocysteine sulfone
-
strong
S-adenosyl-L-homocysteine sulfoxide
-
strong
S-Aristeromycinyl-L-homocysteine
-
-
S-Cytidyl-L-homocysteine
-
weak
S-Inosyl-L-homocysteine
-
weak
S-Tubercidinyl-L-homocysteine
-
strong
S-Uridyl-L-homocysteine
-
weak
A9145C
-
strong
A9145C
-
i.e. amino acid modified structure analogue of adenosyl-L-homocysteine, competitive
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
strong
S-adenosyl-L-homocysteine
-
product inhibition, competitive
sinefungin
-
strong
sinefungin
-
i.e. A9145, competitive
additional information
-
EDTA
-
additional information
-
no inhibition by poly(A), poly(U), poly(C) or poly(G)
-
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C272S/K175C/R209K
2-bromoethylamine reveals 64% target site modification in a overnight reaction at 37°C, unmodified mutant has no detectable methyltransferase activity, whereas the modified protein is active, exhibiting 20-30% of the specific catalytic rate of wild-type
K175C
aziridine reveals 66.7% target site modification in a 4 h, room temperature reaction, equivalent modification level achieved in an overnight incubation using 2-bromoethylamine at 37°C, but protein losses due to aggregation during the modification reaction are, notably, negligible in the lower temperature/shorter duration reactions employed for aziridine
C178S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
C272S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
D182A
-
m7G binding pocket mutant, mutagenesis, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
D182A/E233A
-
m7G binding pocket double mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
E233A
-
m7G binding pocket mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
F180A
-
m7G binding pocket mutant, mutagenesis, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
F180W
-
no apparent defects in catalytic activity
Y22A
-
m7G binding pocket mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
G96D
-
mutation in J3 protein with nucleoside-2-O'-methyltransferase activity evokes a phenotype with abnormally long RNA transcripts analogously to A18 gene-mutation Cts23
G96D
-
double mutant G96D plus Cts23 mutation in gene A18 shows that the J3-mutants serves as an extragenic suppressor of A18-Cts23 mutant
additional information
-
333-codon open-reading frame is cut out and expressed in Escherichia coli, reduced methyltransferase and RNA binding activity
additional information
-
charged amino acids Asp, Glu, His, Lys, Arg are exchanged for Ala by oligonucleotide-directed mutagenesis, glutathione-S-transferase-tagged, 11 of 21 Ala-mutants show reduced activity, 4 show increased activity
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Pugh, C.S.G.; Borchardt, R.T.
Effects of S-adenosylhomocysteine analogues on vaccinia viral messenger ribonucleic acid synthesis and methylation
Biochemistry
21
1535-1541
1982
Vaccinia virus, Vaccinia virus WR
brenda
Ensinger, M.J.; Martin, S.A.; Paoletti, E.; Moss, B.
Modification of the 5-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus
Proc. Natl. Acad. Sci. USA
72
2525-2529
1975
Vaccinia virus, Vaccinia virus WR
brenda
Barbosa, E.; Moss, B.
mRNA(nucleoside-2-)-methyltransferase from vaccinia virus. Purification and physical properties
J. Biol. Chem.
253
7692-7697
1978
Vaccinia virus, Vaccinia virus WR
brenda
Barbosa, E.; Moss, B.
mRNA(nucleoside-2-)-methyltransferase from vaccinia virus. Characteristics and substrate specificity
J. Biol. Chem.
253
7698-7702
1978
Vaccinia virus, Vaccinia virus WR
brenda
Pugh, C.S.G.; Borchardt, R.T.; Stone, H.O.
Sinefungin, a potent inhibitor of virion mRNA(guanine-7-)-methyltransferase, mRNA(nucleoside-2-)-methyltransferase, and viral multiplication
J. Biol. Chem.
253
4075-4077
1978
Vaccinia virus, Vaccinia virus WR
brenda
Schnierle, B.S.; Gershon, P.; Moss, B.
Cap-specific mRNA (nucleoside-O2-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein
Proc. Natl. Acad. Sci. USA
89
2897-2901
1992
Vaccinia virus, Vaccinia virus WR
brenda
Lockless, S.W.; Cheng, H.T.; Hodel, A.E.; Quiocho, F.A.; Gershon, P.D.
Recognition of capped RNA substrates by VP39, the vaccinia virus-encoded mRNA cap-specific 2'-O-methyltransferase
Biochemistry
37
8564-8574
1998
Vaccinia virus
brenda
Schnierle, B.S.; Gershon, P.D.; Moss, B.
Mutational analysis of a multifunctional protein, with mRNA 5' cap-specific (nucleoside-2'-O-)-methyltransferase and 3'-adenylyltransferase stimulatory activities, encoded by vaccinia virus
J. Biol. Chem.
269
20700-20706
1994
Vaccinia virus
brenda
Latner, D.R.; Xiang, Y.; Lewis, J.I.; Condit, J.; Condit, R.C.
The vaccinia virus bifunctional gene J3 (nucleoside-2'-O-)-methyltransferase and poly(A) polymerase stimulatory factor is implicated as a positive transcription elongation factor by two genetic approaches
Virology
269
345-355
2000
Vaccinia virus
brenda
Hu, G.; Tsai, A.L.; Quiocho, F.A.
Insertion of an N7-methylguanine mRNA cap between two coplanar aromatic residues of a cap-binding protein is fast and selective for a positively charged cap
J. Biol. Chem.
278
51515-51520
2003
Vaccinia virus
brenda
Li, C.; Gershon, P.D.
pKa of the mRNA cap-specific 2-O-methyltransferase catalytic lysine by HSQC NMR detection of a two-carbon probe
Biochemistry
45
907-917
2006
Vaccinia virus (P07617)
brenda