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5'-(N7-methylguanosine 5'-triphospho)-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
luciferase mRNA
-
-
?
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
ADP + H2O
AMP + phosphate
less efficient substrate
-
-
?
ApppG + H2O
?
-
unmethylated dinucleotide ApppG is hydrolyzed by the enzyme with greater efficiency than m7GpppG (94.32% hydrolysis after 100 min)
-
-
?
dGDP + H2O
dGMP + phosphate
less efficient substrate
-
-
?
dIDP + H2O
dIMP + phosphate
-
-
-
?
dITP + H2O
IDP + phosphate
less efficient substrate
-
-
?
GDP + H2O
GMP + phosphate
less efficient substrate
-
-
?
GpppA-[16nt mRNA] + H2O
?
-
unmethylated oligonucleotide GpppA-16nt is hydrolyzed by the enzyme with greater efficiency than m7GpppG-[16nt RNA] (89.75% hydrolysis after 60 min)
-
-
?
GpppG + H2O
?
-
unmethylated dinucleotide GpppG is hydrolyzed by the enzyme with greater efficiency than m7GpppG (98.79% hydrolysis after 40 min)
-
-
?
GpppG-[16nt mRNA] + H2O
?
-
unmethylated oligonucleotide GpppG-16nt is hydrolyzed by the enzyme with greater efficiency than m7GpppG-16nt (86.9% hydrolysis after 180 min)
-
-
?
GpppG-[34nt mRNA] + H2O
?
-
81.44% hydrolysis after 5 min
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
ITP + H2O
IDP + phosphate
less efficient substrate
-
-
?
m3-2.2.7GpppG + H2O
?
-
64.96% hydrolysis after 100 min
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
m7G5'ppp5'-NO38 mRNA + H2O
m7GDP + 5'-phospho-NO38 mRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
-
-
?
m7G5'ppp5'-U3 snoRNA + H2O
m7GDP + 5'-phospho-U3 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
-
-
?
m7G5'ppp5'-U3 snoRNA + H2O
m7GDP + U3 snoRNA + H2O
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
-
-
?
m7G5'ppp5'-U8 snomRNA + H2O
m7GDP + 5'-phospho-U8 snomRNA
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
m7GpppA + H2O
?
-
2.57% hydrolysis after 100 min
-
-
?
m7GpppA-[16nt mRNA] + H2O
?
-
45.19% hydrolysis after 240 min
-
-
?
m7GpppG + H2O
?
-
72.97% hydrolysis after 100 min
-
-
?
m7GpppG-[16nt mRNA] + H2O
?
-
94.76% hydrolysis after 180 min
-
-
?
m7GpppG-[34nt mRNA] + H2O
?
-
51.85% hydrolysis after 180 min
-
-
?
m7Gpppm2'-OA + H2O
?
-
1.68% hydrolysis after 100 min
-
-
?
m7Gpppm2'-OA-[16nt mRNA] + H2O
?
-
49.65% hydrolysis after 240 min
-
-
?
m7Gpppm2'-OG + H2O
?
-
76.89% hydrolysis after 100 min
-
-
?
m7Gpppm2'-OG-[16nt mRNA] + H2O
?
-
80.52% hydrolysis after 60 min
-
-
?
m7Gpppm2'-OG-[34nt mRNA] + H2O
?
-
43.86% hydrolysis after 180 min
-
-
?
trimethylguanosine-[16nt mRNA] + H2O
?
-
82.62% hydrolysis after 60 min
-
-
?
XDP + H2O
XMP + phosphate
less efficient substrate
-
-
?
additional information
?
-
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
-
-
-
-
?
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
-
-
-
-
?
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
-
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. mRNA turnover mediated by the decapping complex is required for postembryonic development in Arabidopsis
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. Each component is required for mRNA decapping during postembryonic development
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Dcp2 is involved in mRNA decay
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
decapping of mRNA is a critical step in eukaryotic mRNA turnover
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
mRNA decapping is a critical step in the control of mRNA stability and gene expression
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
a 60 nucleotide element at the 5' end of the mRNA encoding Rrp41 is preferentially bound and decapped by Dcp2. Enhanced decapping of this element is dependent on the structural integrity of its first 33 nt and not its primary sequence. The structure consists of a stem-loop positioned <10 nt from the 5' end of the mRNA
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
hDcp2 is unable to cleave a free cap structure (m7GpppG) generated by P1 nuclease treatment of a cap-labelled RNA. Preferentially cleaves methylated cap structure
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
hDcp2-mediated decapping requires a functional Nudix (nucleotide diphosphate linked to an X moiety) pyrophosphatase motif
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Nudt16 can only function on capped RNA but not N7-methyl cap structure (m7GpppN)
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Dcp2 can only function on capped RNA but not N7-methyl cap structure (m7GpppN)
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Nudt16 can only function on capped RNA but not N7-methyl cap structure (m7GpppN)
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Dcp2 has role in mRNA decay
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
the Dcp2 activity is mediated by the MutT/Nudix domain. A fragment of the yeast Dcp2 protein that contains the MutT/Nudix domain but lacks the non-conserved C-terminal tail is also active in decapping
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
D9 is expressed early in infection and D10 late. It is suggested that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
the mRNA decapping activity of D10 allows vaccinia virus to accelerate degradation of viral and host messages. By degrading host mRNAs, VACV D10 may have an immunomodulatory role
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
cleavage between the alpha- and beta-phosphates of the m7GpppN cap
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
decapping is specific for a methylated cap attached to RNA. D9 differs from D10 in requiring a longer capped RNA substrate for optimal activity. Only trace amounts of the 12- and 24-nt RNA substrates are cleaved. Higher activity with 36-, 48-, or 309-nt RNA substrates
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
RNAs of 24-309 nucleotides are decapped to comparable extents, whereas the cap of a 12-nt RNA is uncleaved. D10 recognizes its substrate through interaction with both cap and RNA moieties. The Nudix/MutT motif of VACV D10 is essential for RNA cap cleavage
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
-
-
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
-
-
?
additional information
?
-
-
X29 has decapping activity and releases m7GDP from full-length U8 RNA. The NUDIX domain in X29 is required for cap cleavage and release of m7GDP from U8 RNA. X29 can cleave the m227G cap present on U8 RNA in vivo
-
-
?
additional information
?
-
-
dinucleotide cap analogs and capped oligonucleotides containing guanine base in the first transcribed nucleotide are more susceptible to enzymatic digestion by the enzyme than their counterparts containing adenine
-
-
-
additional information
?
-
-
no hydrolysis of dinucleotide m7Gpppm7G after 100 min
-
-
-
additional information
?
-
residue Trp43 of subunit Dcp2 is a conserved gatekeeper of the open-to-closed transition that controls the decapping reaction. Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by yeast enhancer of decapping Edc1. Subunit Dcp1 directly contacts the catalytic domain of subunit Dcp2. Coactivation of decapping by Dcp2 is linked to formation of the composite active site
-
-
?
additional information
?
-
-
residue Trp43 of subunit Dcp2 is a conserved gatekeeper of the open-to-closed transition that controls the decapping reaction. Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by yeast enhancer of decapping Edc1. Subunit Dcp1 directly contacts the catalytic domain of subunit Dcp2. Coactivation of decapping by Dcp2 is linked to formation of the composite active site
-
-
?
additional information
?
-
residue Trp43 of subunit Dcp2 is a conserved gatekeeper of the open-to-closed transition that controls the decapping reaction. Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by yeast enhancer of decapping Edc1. Subunit Dcp1 directly contacts the catalytic domain of subunit Dcp2. Coactivation of decapping by Dcp2 is linked to formation of the composite active site
-
-
?
additional information
?
-
X29 has decapping activity and releases m7GDP from full-length U8 RNA. The NUDIX domain in X29 is required for cap cleavage and release of m7GDP from U8 RNA. X29 can cleave the m227G cap present on U8 RNA in vivo
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
-
-
-
-
?
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
-
-
-
-
?
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O
N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
-
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. mRNA turnover mediated by the decapping complex is required for postembryonic development in Arabidopsis
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Dcp2 is involved in mRNA decay
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
decapping of mRNA is a critical step in eukaryotic mRNA turnover
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
mRNA decapping is a critical step in the control of mRNA stability and gene expression
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
Dcp2 has role in mRNA decay
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
D9 is expressed early in infection and D10 late. It is suggested that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
-
the mRNA decapping activity of D10 allows vaccinia virus to accelerate degradation of viral and host messages. By degrading host mRNAs, VACV D10 may have an immunomodulatory role
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zn2+
-
confer only limited hydrolytic capability on hNUDT16. After 30 min incubation of the RNA substrate with the enzyme, only tiny amounts of m7GDP product are observed on the migration profiles
Co2+
-
confer only limited hydrolytic capability on hNUDT16. After 30 min incubation of the RNA substrate with the enzyme, only tiny amounts of m7GDP product are observed on the migration profiles
Co2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher
Co2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher
Mg2+
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
Mg2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Mg2+
contains two Mg2+ ions
Mg2+
conserved glutamate residues E152, E153, and E198 coordinate a magnesium ion through a water mediated contact, while E149 directly contacts the metal
Mg2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Mn2+
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
Mn2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Mn2+
the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
supports D10p catalytic activity, but fails to demonstrate a synergistic effect on the enzyme when tested with Mn2+ ions
IMP
competitive product inhibitor
m7GTP
-
inhibits decapping at large molar ratios relative to capped RNA substrate
Mg2+
-
presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145
Mn2+
-
presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145
N7-methylguanosine 5'-diphosphate
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
N7-methylguanosine 5'-triphosphate
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
poly(A) tail
presence of a poly(A) tail reduces the level of decapping by more than 2fold. The inhibition of decapping is reversed upon the addition of poly(A) competitor
-
m7G5'ppp5'G
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
m7G5'ppp5'G
-
inhibits decapping at large molar ratios relative to capped RNA substrate
m7GDP
-
inhibits decapping at large molar ratios relative to capped RNA substrate
m7GDP
although product inhibition by released m7GDP may occur, the amount of m7GDP released from RNA by X29 in these decapping reactions is well below the amount found to inhibit X29 decapping activity in the assay
uncapped RNA
-
D9 differs from D10 in having greater sensitivity to inhibition by uncapped RNA
-
uncapped RNA
-
high concentrations of uncapped RNA are inhibitory
-
additional information
(m7GpppG) is unable to inhibit competitively the hDcp2 reaction
-
additional information
-
(m7GpppG) is unable to inhibit competitively the hDcp2 reaction
-
additional information
-
Ca2+ ions can not support D10p activity and does not produce a synergistic activation ofD10p in the presence of Mn2+
-
additional information
-
even higher concentrations of unmethylated analogs do not inhibit
-
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5'-(n7-methylguanosine 5'-triphospho)-[mrna] hydrolase deficiency
CAG RNAs induce DNA damage and apoptosis by silencing NUDT16 expression in polyglutamine degeneration.
Infections
Virus-induced translational arrest through 4EBP1/2-dependent decay of 5'-TOP mRNAs restricts viral infection.
Mental Retardation, X-Linked
Identification of an mRNA-decapping regulator implicated in X-linked mental retardation.
Muscular Atrophy, Spinal
A library approach to rapidly discover photoaffinity probes of the mRNA decapping scavenger enzyme DcpS.
Poxviridae Infections
The D10 decapping enzyme of vaccinia virus contributes to decay of cellular and viral mRNAs and to virulence in mice.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Epigenetic loss of the RNA decapping enzyme NUDT16 mediates C-MYC activation in T-cell acute lymphoblastic leukemia.
Thyroid Neoplasms
Comprehensive Analysis of the Functions and Prognostic Value of RNA-Binding Proteins in Thyroid Cancer.
Vaccinia
Characterization of a vaccinia virus mutant with a deletion of the D10R gene encoding a putative negative regulator of gene expression.
Vaccinia
Characterization of the vaccinia virus D10 decapping enzyme provides evidence for a two-metal-ion mechanism.
Vaccinia
Down regulation of gene expression by the vaccinia virus D10 protein.
Vaccinia
Insights into the molecular determinants involved in cap recognition by the vaccinia virus D10 decapping enzyme.
Vaccinia
Investigation of IRES Insertion into the Genome of Recombinant MVA as a Translation Enhancer in the Context of Transcript Decapping.
Vaccinia
The D10 decapping enzyme of vaccinia virus contributes to decay of cellular and viral mRNAs and to virulence in mice.
Vaccinia
Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression.
Virus Diseases
Characterization of a vaccinia virus mutant with a deletion of the D10R gene encoding a putative negative regulator of gene expression.
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malfunction
no obvious phenotypic difference or differences in fertility, life span, or litter size are detected between the wild type animals and Dcp2b/b mice (mice containing a homozygous insertion of the beta-geo gene as Dcp2beta/beta)
malfunction
-
null mutants of DCP1 accumulate capped mRNAs with a reduced degradation rate. Lethal phenotype at the seedling cotyledon stage, with disorganized veins, swollen root hairs, and altered epidermal cell morphology
malfunction
-
enzyme-deficient viruses are attenuated in mice. Decapping-deficient vaccinia virus also potently reduces tumor growth in a human hepatocellular carcinoma xenograft model
malfunction
-
reduction of enzyme protein levels in MCF-7 cells promotes increased cell migration and corresponding enhanced filopodia extensions. Enzyme depletion elevates RNA and protein expression of integrin beta6 and fibronectin, which in turn increases MCF-7 cell motility
physiological function
-
D9 is expressed early in infection and D10 late. It is suggested that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner
physiological function
-
mRNA decapping is a critical step in the control of mRNA stability and gene expression
physiological function
Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
physiological function
Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
physiological function
-
the mRNA decapping activity of D10 allows Vaccinia virus to accelerate degradation of viral and host messages. By degrading host mRNAs, VACV D10 may have an immunomodulatory role. Although it may seem self-destructive for a virus to encode a decapping and a capping enzyme, accelerated mRNA turnover helps eliminate competing host mRNAs and allows stagespecific synthesis of viral proteins
physiological function
the presence or absence of detectable Dcp2 does not appreciably alter stability of the transfected RNA and suggests Dcp2 may not be involved in bulk mRNA decapping in cells. Dcp2 appears to be a minor contributor to mRNA stability and raises the intriguing possibility for the presence of a Dcp2-independent decapping activity in mammalian cells
physiological function
embryonic fibroblast cells with reduced Dcp2 levels contain significantly elevated levels of mRNAs encoding proteins involved in the type I IFN response. Both IRF-7 mRNA and protein are increased in cells with reduced Dcp2 levels. The increase in IRF-7 mRNA within the background of reduced Dcp2 levels is attributed to a stabilization of the IRF-7 mRNA, suggesting that Dcp2 normally modulates IRF-7 mRNA stability
physiological function
many long noncoding RNAs degraded by DCP2 are expressed proximal to inducible genes. Of these, several genes required for galactose utilization are associated with long noncoding RNAs that have expression patterns inversely correlated with their mRNA counterpart. Decapping of these lncRNAs is critical for rapid and robust induction of GAL gene expression
physiological function
-
the enzyme is a modulator of MCF-7 breast cancer cell migration
physiological function
-
the enzyme regulates mRNA stability in cells
physiological function
-
the enzyme regulates mRNA stability in cells
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A22V
the differences in the kinetic parameters caused by the A22V mutation are small (less than a factor 2)
E148Q
mutant enzyme is as stable as the wild-type enzyme
E76Q
-
mutation totally abolishes the decapping activity under the standard assaying condition
E79Q
-
mutation decreases the decapping activity of the enzyme
E80Q
-
mutation totally abolishes the decapping activity under the standard assaying condition
R75L
-
the mutant displays a weaker capability of hydrolysis
E153Q
mutant has 3 molecules in the asymmetric unit. There is clear electron density for an octahedrally coordinated Mg2+ in the structure, similar to wild-type. Mutant is severely catalytically compromised and displays a linear dependence on pH over the range studied (pH 79.5)
E198Q
mutant lacks clear density for a metal ion in the active site and fails to crystallize in the presence of any divalent cation
W50A
Mutation in subunit Dcp2. While the wild-type Dcp1-Dcp2 complex is stimulated by enhancer of decapping Edc1CTR by a factor of 13, it only enhances catalysis in the W50A mutant by a factor of three. Coactivation of decapping by Dcp2 is linked to formation of the composite active site
E132A
-
7.8% of wild-type activity. The E132A mutant shows a 5fold reduced affinity for Mg2+, but retains a Mn2+ affinity similar to that of the wild type
E141A
-
10% of wild-type activity. The E141A mutant demonstrates only slight variations in both Mg2+ and Mn2+ binding
E141Q
-
inactive mutant enzyme
E144Q/E145Q
-
inactive mutant enzyme
E145A
-
12.2% of wild-type activity. the E145A mutant shows 2-fold reduced affinity for Mg2+ and 6-fold reduced Mn2+ binding
E150Q
mutant protein is inactive under all conditions
E89Q
mutant protein is inactive under all conditions
E92Q
mutant displays weak decapping activity under the standard decapping conditions in both Mg2+ and Mn2+, a significant increase in hydrolysis in the presence of higher concentrations of metal
E92Q/E93Q
mutation displays less than 5% decapping activity in Mn2+ under the optimized decapping conditions. A 10fold increase in the amount of metal present in the reaction (to 1 mM Mn2+) only marginally increases the efficiency of cap hydrolysis
E93Q
mutation displays less than 5% decapping activity in Mn2+ under the optimized decapping conditions. A 10fold increase in the amount of metal present in the reaction (to 1 mM Mn2+) only marginally increases the efficiency of cap hydrolysis
additional information
-
decapping actiovity is abolished by point mutations in the Nudix hydrolase motif
W43A
mutation at Trp43 blocks kinetic stimulation by subunit Dcp1
W43A
-
mutation at Trp43 blocks kinetic stimulation by subunit Dcp1
-
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Ghosh, T.; Peterson, B.; Tomasevic, N.; Peculis, B.A.
Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme
Mol. Cell
13
817-828
2004
Homo sapiens, Xenopus laevis (Q6TEC1)
brenda
Zhang, J.; Gao, F.; Zhang, Q.; Chen, Q.; Qi, J.; Yan, J.
Crystallization and crystallographic analysis of human NUDT16
Acta Crystallogr. Sect. F
64
639-640
2008
Homo sapiens
brenda
Soulire, M.F.; Perreault, J.P.; Bisaillon. M.
Characterization of the vaccinia virus D10 decapping enzyme provides evidence for a two-metal-ion mechanism
Biochem. J.
420
27-35
2009
Vaccinia virus
brenda
van Dijk, E.; Cougot, N.; Meyer, S.; Babajko, S.; Wahle, E.; Sraphin, B.
Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
EMBO J.
21
6915-6924
2002
Saccharomyces cerevisiae (P53550), Saccharomyces cerevisiae, Homo sapiens (Q8IU60), Homo sapiens
brenda
Peculis, B.A.; Reynolds, K.; Cleland, M.
Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)
J. Biol. Chem.
282
24792-24805
2007
Xenopus laevis (Q6TEC1), Homo sapiens (Q96DE0), Homo sapiens
brenda
Parrish, S.; Moss, B.
Characterization of a second vaccinia virus mRNA-decapping enzyme conserved in poxviruses
J. Virol.
81
12973-12978
2007
Vaccinia virus
brenda
Lykke-Andersen, J.
Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay
Mol. Cell. Biol.
22
8114-8121
2002
Homo sapiens (Q8IU60), Homo sapiens
brenda
Song, M.G.; Li, Y.; Kiledjian, M.
Multiple mRNA decapping enzymes in mammalian cells
Mol. Cell.
40
423-432
2010
Mus musculus (Q6P3D0), Mus musculus (Q9CYC6), Mus musculus, Homo sapiens (Q8IU60), Homo sapiens (Q96DE0), Homo sapiens
brenda
Li, Y.; Ho, E.S.; Gunderson, S.I.; Kiledjian, M.
Mutational analysis of a Dcp2-binding element reveals general enhancement of decapping by 5'-end stem-loop structures
Nucleic Acids Res.
37
2227-2237
2009
Homo sapiens
brenda
Xu, J.; Yang, J.Y.; Niu, Q.W.; Chua, N.H.
Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development
Plant Cell
18
3386-3398
2006
Arabidopsis thaliana
brenda
Parrish, S.; Resch, W.; Moss, B.
Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression
Proc. Natl. Acad. Sci. USA
104
2139-2144
2007
Vaccinia virus
brenda
Wang, Z.; Jiao, X.; Carr-Schmid, A.; Kiledjian, M.
The hDcp2 protein is a mammalian mRNA decapping enzyme
Proc. Natl. Acad. Sci. USA
99
12663-12668
2002
Homo sapiens (Q8IU60), Homo sapiens
brenda
Lu, G.; Zhang, J.; Li, Y.; Li, Z.; Zhang, N.; Xu, X.; Wang, T.; Guan, Z.; Gao, G.F.; Yan, J.
hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA
Protein Cell
2
64-73
2011
Homo sapiens
brenda
Liu, S.W.; Jiao, X.; Liu, H.; Gu, M.; Lima, C.D.; Kiledjian, M.
Functional analysis of mRNA scavenger decapping enzymes
RNA
10
1412-1422
2004
Homo sapiens (Q8IU60)
brenda
Scarsdale, J.N.; Peculis, B.A.; Wright, H.T.
Crystal structures of U8 snoRNA decapping nudix hydrolase, X29, and its metal and cap complexes
Structure
14
331-343
2006
Xenopus laevis (Q6TEC1), Xenopus laevis
brenda
Fromm, S.; Truffault, V.; Kamenz, J.; Braun, J.; Hoffmann, N.; Izaurralde, E.; Sprangers, R.
The structural basis of Edc3-and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex
EMBO J.
31
279-290
2012
Schizosaccharomyces pombe (O13828), Schizosaccharomyces pombe ATCC 24843 (O13828)
brenda
Li, Y.; Dai, J.; Song, M.; Fitzgerald-Bocarsly, P.; Kiledjian, M.
Dcp2 decapping protein modulates mRNA stability of the critical interferon regulatory factor (IRF) IRF-7
Mol. Cell. Biol.
32
1164-1172
2012
Mus musculus (Q9CYC6)
brenda
Geisler, S.; Lojek, L.; Khalil, A.; Baker, K.; Coller, J.
Decapping of long noncoding RNAs regulates inducible genes
Mol. Cell.
45
279-291
2012
Saccharomyces cerevisiae (P53550)
brenda
Floor, S.; Borja, M.; Gross, J.
Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan
Proc. Natl. Acad. Sci. USA
109
2872-2877
2012
Schizosaccharomyces pombe (O13828), Schizosaccharomyces pombe, Saccharomyces cerevisiae (P53550), Saccharomyces cerevisiae, Schizosaccharomyces pombe ATCC 24843 (O13828)
brenda
Aglietti, R.A.; Floor, S.N.; McClendon, C.L.; Jacobson, M.P.; Gross, J.D.
Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2
Structure
21
1571-1580
2013
Saccharomyces cerevisiae (P53550)
brenda
Burgess, H.M.; Pourchet, A.; Hajdu, C.H.; Chiriboga, L.; Frey, A.B.; Mohr, I.
Targeting poxvirus decapping enzymes and mRNA decay to generate an effective oncolytic virus
Mol. Ther. Oncolytics
8
71-81
2018
Vaccinia virus
brenda
Tresaugues, L.; Lundbaeck, T.; Welin, M.; Flodin, S.; Nyman, T.; Silvander, C.; Graeslund, S.; Nordlund, P.
Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate
PLoS ONE
10
e0131507
2015
Homo sapiens (Q96DE0), Homo sapiens
brenda
Grudzien-Nogalska, E.; Jiao, X.; Song, M.G.; Hart, R.P.; Kiledjian, M.
Nudt3 is an mRNA decapping enzyme that modulates cell migration
RNA
22
773-781
2016
Homo sapiens
brenda
Grzela, R.; Nasilowska, K.; Lukaszewicz, M.; Tyras, M.; Stepinski, J.; Jankowska-Anyszka, M.; Bojarska, E.; Darzynkiewicz, E.
Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides
RNA
24
633-642
2018
Homo sapiens
brenda
Grudzien-Nogalska, E.; Kiledjian, M.
New insights into decapping enzymes and selective mRNA decay
Wiley Interdiscip. Rev. RNA
8
e1379
2017
Saccharomyces cerevisiae, Homo sapiens
brenda