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Information on EC 2.3.1.258 - N-terminal methionine Nalpha-acetyltransferase NatE
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2.3.1.258 N-terminal methionine Nalpha-acetyltransferase NatEIUBMB Comments
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nalpha-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.
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Word Map
- 2.3.1.258
-
auxiliary
-
nt-acetylation
-
bisubstrate
- n-acetyltransferase
-
n-termini
-
drug-induced
-
tunnel
-
chromatid
-
sister
-
acetylome
-
nalpha-terminal
-
co-translationally
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
naa50, hnata, hnaa50, naa50/san, scnaa50, nata/naa50 complex, n-terminal acetyltransferase e, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ARD1
EC 2.3.1.88
-
-
formerly, part transferred
-
NAA10
NAA15
Naa50
Naa50p
Nalpha-acetyltransferase
NAT1
NAT5
NatA
NatA/Naa50 complex
NatE
SAN
Naa50
-
-
-
-
NAT5
-
-
-
-
SAN
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein] + CoA
(1)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
(5)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
(7)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-seryl-[protein] + CoA
(2)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-threonyl-[protein] + CoA
(4)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
(8)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
(3)
-
-
-
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
hNaa50p utilizes an ordered bi bi reaction of the Theorell-Chance type, substarte binding study and dynamics using NMR spectroscopy. Acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site. Addition of peptide in the absence of acetyl-CoA does not alter the structure of the protein
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(6)
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nalpha-acetyltransferase
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nalpha-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
-
best substrate
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-seryl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-threonyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRP
acetyl-CoA + Nalpha-acetyl-MLGPEGGRWGRPVGRRRRP
-
-
-
?
acetyl-CoA + MMAA
Nalpha-acetyl-MMAA + CoA
-
substrate with highest catalytic efficiency
-
-
?
acetyl-CoA + N-terminal L-methionyl-[ARYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[ARYFRR]
DP9 peptide (MARYFRR) is a substrate of NatE, a synthetic peptide
-
-
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
-
-
-
ir
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
peptide substrate binding structure, overview
-
-
?
additional information
?
-
-
ectopically expressed hNaa50 results, predominantly, in the N-terminal-acetylation of N-terminal Met (iMet) starting N-termini, including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr N-termini. Presence of a kinetic competition between Naa50 and Met-aminopeptidases
-
-
?
additional information
?
-
Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
-
-
?
additional information
?
-
-
Naa50p also possesses Nepsilon-autoacetylation activity
-
-
?
additional information
?
-
Naa50p also possesses Nepsilon-autoacetylation activity
-
-
?
additional information
?
-
no activity with peptides SESSRRR, SYSMRRR, and DDIARRR
-
-
?
additional information
?
-
preferably the enzyme acetylates oligopeptides with N-termini Met-Leu-Xxx-Pro. Furthermore, the enzyme autoacetylates lysines 34, 37, and 140 in vitro as well as histone 4
-
-
?
additional information
?
-
-
the enzyme acetylates all MXAA peptides except for MPAA
-
-
?
additional information
?
-
complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
-
-
-
additional information
?
-
-
complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
-
-
-
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES. RimIMtb acetylates DP9 (NatE substrate) 2.1fold better than DPC (NatA substrate). RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
-
-
-
additional information
?
-
-
potential substrates that are less acetylated in strains lacking isoform Naa50 are: vacuolar morphogenesis protein 7, nuclear cap-binding protein subunit 2, 60S ribosomal protein L16-A, aromatic amino acid aminotransferase 1, tRNA guanosine-2'-O-methyltransferase TRM3, low specificity L-threonine aldolase
-
-
?
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
-
best substrate
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-seryl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-threonyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
SpNaa50 maintains the ability to co-migrate with SpNatA in sizing buffer with NaCl concentration as high as 1 M
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CoA
competitive product inhibition; product inhibition, competitive versus acetyl-CoA, noncompetitive against peptide substrate well in line with a ternary complex mechanism. The non-competitive inhibition pattern observed when CoA is tested against peptide as variable substrate and at fixed concentrations of acetyl-CoA also rules out a ping-pong mechanism
HYPK
UniProt ID Q9NX55, a protein with intrinsic NAA10 catalytic subunit inhibitory activity. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex. hNatE displays an about 8.6fold decrease of Km, and an about 1.1fold decrease of kcat, with an overall 7.7fold increase of catalytic efficiency, compared to hNAA50. In the presence HYPK, hNatE displays an about 1.3fold decrease in Km, and an about 3.8fold decrease in kcat, with an overall 2.9fold decrease in catalytic efficiency compared to hNatE alone. The hNatE/HYPK structure reveals a negative cooperative mechanism. Over the HYPK and hNatA interaction interface within the tetrameric complex, polar interactions between HYPK-Glu74 and hNAA15-Tyr158, between the backbone carbonyl of HYPK-Thr100 and hNAA15-Lys687, between the backbone carbonyl of HYPK-Asn129 and hNAA15-Arg697, and between HYPK-Asn129 and hNAA15-Lys696 are observed
-
additional information
NAA50 and HYPK each contribute to NAA10 activity inhibition through structural alteration of the NAA10 substrate-binding site. NAA50 activity is increased through NAA15 tethering, but is inhibited by HYPK through structural alteration of the NatE substrate-binding site. hNAA50 and HYPK inhibit hNatA activity, and HYPK is dominant. The hNatE structure reveals molecular basis for enzyme crosstalk
-
additional information
-
NAA50 and HYPK each contribute to NAA10 activity inhibition through structural alteration of the NAA10 substrate-binding site. NAA50 activity is increased through NAA15 tethering, but is inhibited by HYPK through structural alteration of the NatE substrate-binding site. hNAA50 and HYPK inhibit hNatA activity, and HYPK is dominant. The hNatE structure reveals molecular basis for enzyme crosstalk
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NAA50 activity is increased through NAA15 tethering. hNatA significantly enhances the catalytic efficiency of hNatE
-
additional information
-
NAA50 activity is increased through NAA15 tethering. hNatA significantly enhances the catalytic efficiency of hNatE
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0962
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNatE, pH 8.5, 37°C
0.8315
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNaa50, pH 8.5, 37°C
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
binding kinetics of hNaa50 and hNatA, Naa50 tightly binds to NatA
-
additional information
additional information
-
binding kinetics of hNaa50 and hNatA, Naa50 tightly binds to NatA
-
additional information
additional information
binding kinetics of ScNaa50 and ScNatA
-
additional information
additional information
-
binding kinetics of ScNaa50 and ScNatA
-
additional information
additional information
-
binding kinetics of SpNaa50 and SpNatA, Naa50 tightly binds to NatA
-
additional information
additional information
kinetic analysis of wild-type enzyme and enzyme mutant MtRimIC21A4-153
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0515
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNatE, pH 8.5, 37°C
0.0575
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNaa50, pH 8.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.069
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNaa50, pH 8.5, 37°C
0.535
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNatE, pH 8.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00227
CoA
with acetyl-CoA, pH 7.4, temperature not specified in the publication
0.00277
CoA
with peptide, pH 7.4, temperature not specified in the publication
0.067
desulfo-CoA
with acetyl-CoA, pH 7.4, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1300
about, purified recombinant RimI, NatE substrate N-terminal L-methionyl-[ARYFRR], pH 8.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
UniProt
NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
UniProt
NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
UniProt
NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
evolution
-
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
evolution
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
evolution
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
evolution
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
evolution
-
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
evolution
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
evolution
-
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
-
evolution
-
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
-
evolution
-
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
-
evolution
-
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
-
evolution
-
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
-
evolution
-
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
-
evolution
-
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
-
evolution
-
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
-
malfunction
-
depletion of Naa50 in HeLa cells causes cohesion defects in interphase
malfunction
enzyme depletion causes premature sister chromatid separation in HeLa cells
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
malfunction
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
malfunction
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association. Deletion of ScNaa50 shows no phenotype, while Naa50 knockout in higher organisms has been shown to perturb sister chromatid cohesion
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
-
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
-
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association. Deletion of ScNaa50 shows no phenotype, while Naa50 knockout in higher organisms has been shown to perturb sister chromatid cohesion
-
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
physiological function
-
Naa50 promotes sister-chromatid cohesion and promotes binding of sororin to cohesin
physiological function
-
Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion during Drosophila wing development. The enzyme is required for the correct interaction between Scc1 and Smc3
physiological function
the acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner. The enzyme is specifically required for the maintenance of the centromeric cohesion in mitosis
physiological function
-
the gene san is required in vivo for normal mitosis of different types of somatic cells. In addition, it is also important for the correct resolution of chromosomes. During oogenesis the gene san is not required for germ line mitosis
physiological function
enzyme complex NatE co-translationally acetylates the N-terminus of half the proteome to mediate diverse biological processes, including protein half-life, localization, and interaction. The complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
physiological function
-
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
physiological function
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
physiological function
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is estimated to affect up to 90% of human proteins and influences their folding, localization, complex formation, and degradation, along with a variety of cellular functions ranging from apoptosis to gene regulation. NTA is an irreversible protein modification
physiological function
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
physiological function
-
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
physiological function
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
physiological function
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
physiological function
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
physiological function
-
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
-
physiological function
-
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
-
physiological function
-
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
-
physiological function
-
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
-
physiological function
-
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
-
physiological function
-
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
-
physiological function
-
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
-
physiological function
-
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
-
physiological function
-
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
-
physiological function
-
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
-
additional information
structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
the human N-terminal acetyltransferase E (NatE) contains NAA10 and NAA50 as catalytic subunits, and NAA15 auxiliary as subunit and associates with HYPK, a protein with intrinsic NAA10 inhibitory activity. hNatE and inhibitor HYPK form a tetrameric complex. Analysis of the molecular basis for how NatE and HYPK cooperate, cryo-EM structures of human NatE and NatE/HYPK complexes, overview. NAA50 and HYPK exhibit negative cooperative binding to NAA15 in vitro and in human cells by inducing NAA15 shifts in opposing directions. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex
additional information
-
the human N-terminal acetyltransferase E (NatE) contains NAA10 and NAA50 as catalytic subunits, and NAA15 auxiliary as subunit and associates with HYPK, a protein with intrinsic NAA10 inhibitory activity. hNatE and inhibitor HYPK form a tetrameric complex. Analysis of the molecular basis for how NatE and HYPK cooperate, cryo-EM structures of human NatE and NatE/HYPK complexes, overview. NAA50 and HYPK exhibit negative cooperative binding to NAA15 in vitro and in human cells by inducing NAA15 shifts in opposing directions. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
additional information
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
additional information
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
-
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
-
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
-
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
-
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA
-
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
-
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). NAT5_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
176
0
19727
Swiss-Prot
other Location (Reliability: 2)
SAN_DROME
184
0
20994
Swiss-Prot
other Location (Reliability: 1)
NAA50_BOVIN
169
0
19398
Swiss-Prot
other Location (Reliability: 2)
NAA50_DANRE
168
0
19195
Swiss-Prot
other Location (Reliability: 2)
NAA50_HUMAN
169
0
19398
Swiss-Prot
other Location (Reliability: 2)
NAA50_MOUSE
169
0
19414
Swiss-Prot
other Location (Reliability: 2)
NAA50_PONAB
169
0
19398
Swiss-Prot
other Location (Reliability: 2)
NAA50_XENLA
170
0
19499
Swiss-Prot
other Location (Reliability: 2)
NAA50_XENTR
169
0
19412
Swiss-Prot
other Location (Reliability: 2)
RIMI_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
158
0
17389
Swiss-Prot
-
NAT_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
167
0
19448
Swiss-Prot
-
NAT_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
168
0
19537
Swiss-Prot
-
NAT_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
167
0
19276
Swiss-Prot
-
A0A6J8EMY1_MYTCO
167
0
19397
TrEMBL
other Location (Reliability: 2)
A0A7R8H892_LEPSM
120
0
13965
TrEMBL
other Location (Reliability: 1)
A0A484IEG4_9ARCH
171
0
19557
TrEMBL
-
A0A2K5APB8_9ARCH
169
0
19580
TrEMBL
-
A0A5B6YRB5_DAVIN
117
0
13353
TrEMBL
other Location (Reliability: 4)
A0A7R8HA99_LEPSM
109
0
12250
TrEMBL
Mitochondrion (Reliability: 3)
A0A5B6YRQ1_DAVIN
164
0
18510
TrEMBL
other Location (Reliability: 2)
A0A812AZ54_SEPPH
349
3
39830
TrEMBL
other Location (Reliability: 2)
A0A812F1Z3_9ARCH
169
0
19644
TrEMBL
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15
additional information
secondary structure prediction of MtRimI, overview
additional information
-
secondary structure prediction of MtRimI, overview
-
additional information
-
secondary structure prediction of MtRimI, overview
-
additional information
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
-
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
-
additional information
-
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to a native substrate peptide fragment (MLGPEGGRWG) and CoA, hanging drop vapor diffusion method, using 16% (w/v) PEG 8000, 20% (v/v) glycerol, and 40 mM potassium phosphate (monobasic, pH 5.0)
hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M sodium formate
-
Naa50p bound to a native substrate peptide fragment and CoA, hanging drop vapor diffusion method, mixing of 12 mg/ml protein in 25 mM HEPES, pH 7.5, 100 mM NaCl, and 10mM dithiothreitol, with peptide MLGPEGGRWG solution, and crystallization solution, containing 16% PEG 8000, 20% glycerol, and 40 mM potassium phosphate, pH 5.0, in a 1:3:3 molar ratio, 20°C, 1-3 days, X-ray diffraction structure determination and analysis at 2.75 A resolution
purified hNatE and hNatE in complex with inhibitor HYPK, X-ray diffraction structure determination and analysis at 4.5-5.0 A resolution
NatA/Naa50 complex, i.e. NatE, including full-length ScNaa15 (residues 1-854), C-terminally truncated ScNaa10 (1-226 out of 238 total residues), and full-length ScNaa50 (residues 1-176), in the presence of inositol hexaphosphate (IP6) and bi-substrate analogues for both Naa10 and Naa50, X-ray diffraction structure determination and analysis
purified recombinant ScNatA/Naa50 complex, X-ray diffraction structure determination and analysis at 2.7 A resolution
NatA/Naa50 complex, i.e. NatE, X-ray diffraction structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F27A
F35A
H112A
H112F
I142A
L814P
site-directed mutagenesis, the hNAA15 mutant is defective for HYPK inhibition and reduces hNatA thermostability, hNAA10 binding is not affected
P28A
T406Y
site-directed mutagenesis, the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected
V29A
Y124F
the mutant shows decreased activity compared to the wild type enzyme
Y139A
Y31A
Y73A
Y73F
additional information
I142A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P28A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V29A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
additional information
-
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
additional information
generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
-
generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
-
additional information
-
generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
-
additional information
N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae
additional information
-
N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae
additional information
-
N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae
-
additional information
-
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
additional information
-
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
-
additional information
-
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme RimI from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant GST-tagged full-length Naa50p from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography and cleavage of the GST-tag by TEV protease, followed by ion exchange chromatography and gel filtration
recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration
recombinant GST-tagged SpNatA and SpNaa50 from Escherichia coli by glutathione affinity chromatography and gel filtration, SpNaa50 maintains the ability to co-migrate with SpNatA in sizing buffer with NaCl concentration as high as 1 M
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant hNaa15 mutants, hNaa50, and hNatA by affinity chromatography and gel filtration
recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration
recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression of GST-tagged full-length Naa50p with a TEV protease-cleavable site in Escherichia coli strain BL21(DE3)
gene rimI, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Rv3420c or rimI, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli
recombinant expression of hNaa15 mutants in HeLa cells, recombinant expression of N-terminally His-tagged NatA in Spodoptera frugiperda Sf9 cells, recombinant expression of His-tagged hNaa50 in Escherichia coli strain Rosetta (DE3)pLysS and strain BL21(DE3), coexpression of tagged HYPK
recombinant expression ofthe NatA/Naa50 complex, i.e. NatE, in Escherichia coli
recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
recombinant overexpression of N-terminally GST-tagged SpNatA and SpNaa50 in Escherichia coli
-
recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
Naa50p is a therapeutic anti-cancer target, the structure of the ternary Naa50p complex also provides a molecular scaffold for the design of NAT-specific small molecule inhibitors with possible therapeutic applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arnesen, T.; Anderson, D.; Torsvik, J.; Halseth, H.B.; Varhaug, J.E.; Lillehaug, J.R.
Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex
Gene
371
291-295
2006
Homo sapiens (Q9GZZ1)
Liszczak, G.; Arnesen, T.; Marmorsteins, R.
Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation
J. Biol. Chem.
286
37002-37010
2011
Homo sapiens, Homo sapiens (Q9GZZ1)
Evjenth, R.H.; Brenner, A.K.; Thompson, P.R.; Arnesen, T.; Fr?ystein, N.A.; Lillehaug, J.R.
Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study
J. Biol. Chem.
287
10081-10088
2012
Homo sapiens, Homo sapiens (Q9GZZ1)
Van Damme, P.; Hole, K.; Gevaert, K.; Arnesen, T.
N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases
Proteomics
15
2436-2446
2015
Homo sapiens, Saccharomyces cerevisiae
Pimenta-Marques, A.; Tostoes, R.; Marty, T.; Barbosa, V.; Lehmann, R.; Martinho, R.
Differential requirements of a mitotic acetyltransferase in somatic and germ line cells
Dev. Biol.
323
197-206
2008
Drosophila melanogaster
Evjenth, R.; Hole, K.; Karlsen, O.; Ziegler, M.; Amesen, T.; Lillehaug, J.
Human Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
J. Biol. Chem.
284
31122-31129
2009
Homo sapiens (Q9GZZ1)
Rong, Z.; Ouyang, Z.; Magin, R.S.; Marmorstein, R.; Yu, H.
Opposing functions of the N-terminal acetyltransferases Naa50 and NatA in sister-chromatid cohesion
J. Biol. Chem.
291
19079-19091
2016
Homo sapiens
Reddi, R.; Saddanapu, V.; Chinthapalli, D.; Sankoju, P.; Sripadi, P.; Addlagatta, A.
Human Naa50 protein displays broad substrate specificity for amino-terminal acetylation: Detailed structural and biochemical analysis using tetrapeptide library
J. Biol. Chem.
291
20530-20538
2016
Homo sapiens
Hou, F.; Chu, C.; Kong, X.; Yokomori, K.; Zou, H.
The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner
J. Cell Biol.
177
587-597
2007
Homo sapiens (Q9GZZ1)
Ribeiro, A.L.; Silva, R.D.; Foyn, H.; Tiago, M.N.; Rathore, O.S.; Arnesen, T.; Martinho, R.G.
Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion
Sci. Rep.
6
39118
2016
Drosophila melanogaster
Hou, M.; Zhuang, J.; Fan, S.; Wang, H.; Guo, C.; Yao, H.; Lin, D.; Liao, X.
Biophysical and functional characterizations of recombinant RimI acetyltransferase from Mycobacterium tuberculosis
Acta Biochim. Biophys. Sin. (Shanghai)
51
960-968
2019
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis ATCC 25618 (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32)
Deng, S.; McTiernan, N.; Wei, X.; Arnesen, T.; Marmorstein, R.
Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
Nat. Commun.
11
818
2020
Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Homo sapiens
Pathak, D.; Bhat, A.; Sapehia, V.; Rai, J.; Rao, A.
Biochemical evidence for relaxed substrate specificity of Nalpha-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis
Sci. Rep.
6
28892
2016
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis ATCC 25618 (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32)
Lyon, G.
From molecular understanding to organismal biology of N-terminal acetyltransferases
Structure
27
1053-1055
2019
Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Saccharomyces cerevisiae (Q08689 AND P41227 AND P12945), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q08689 AND P41227 AND P12945), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972, Schizosaccharomyces pombe ATCC 24843
Deng, S.; Magin, R.; Wei, X.; Pan, B.; Petersson, E.; Marmorstein, R.
Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex
Structure
27
1057-1070.e4
2019
Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Homo sapiens, Saccharomyces cerevisiae (Q08689 AND P07347 AND P12945), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q08689 AND P07347 AND P12945), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972, Schizosaccharomyces pombe ATCC 24843
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