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Literature summary for 2.3.1.258 extracted from
- Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex (2019), Structure, 27, 1057-1070.e4 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Homo sapiens |
| recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system | Saccharomyces cerevisiae |
| recombinant overexpression of N-terminally GST-tagged SpNatA and SpNaa50 in Escherichia coli | Schizosaccharomyces pombe |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant ScNatA/Naa50 complex, X-ray diffraction structure determination and analysis at 2.7 A resolution | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex | Schizosaccharomyces pombe |
| additional information | recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | binding kinetics of hNaa50 and hNatA, Naa50 tightly binds to NatA | Homo sapiens | |
| additional information | - |
additional information | binding kinetics of ScNaa50 and ScNatA | Saccharomyces cerevisiae | |
| additional information | - |
additional information | binding kinetics of SpNaa50 and SpNatA, Naa50 tightly binds to NatA | Schizosaccharomyces pombe |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | SpNaa50 maintains the ability to co-migrate with SpNatA in sizing buffer with NaCl concentration as high as 1 M | Schizosaccharomyces pombe |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9GZZ1 AND P41227 AND Q9BXJ9 | NatE complex subunits Naa50, Naa10, and Naa15 | - |
| Saccharomyces cerevisiae | Q08689 AND P07347 AND P12945 | NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1) | - |
| Saccharomyces cerevisiae ATCC 204508 | Q08689 AND P07347 AND P12945 | NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1) | - |
| Schizosaccharomyces pombe | - |
- |
- |
| Schizosaccharomyces pombe 972 | - |
- |
- |
| Schizosaccharomyces pombe ATCC 24843 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration | Homo sapiens |
| recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration | Saccharomyces cerevisiae |
| 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 | Schizosaccharomyces pombe |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ARD1 | - |
Schizosaccharomyces pombe |
| ARD1 | - |
Saccharomyces cerevisiae |
| hNaa50 | - |
Homo sapiens |
| hNatA | - |
Homo sapiens |
| NAA10 | - |
Schizosaccharomyces pombe |
| NAA10 | - |
Homo sapiens |
| NAA10 | - |
Saccharomyces cerevisiae |
| NAA15 | - |
Schizosaccharomyces pombe |
| NAA15 | - |
Homo sapiens |
| NAA15 | - |
Saccharomyces cerevisiae |
| Naa50 | - |
Schizosaccharomyces pombe |
| Naa50 | - |
Homo sapiens |
| Naa50 | - |
Saccharomyces cerevisiae |
| NAT1 | - |
Schizosaccharomyces pombe |
| NAT1 | - |
Saccharomyces cerevisiae |
| NatA/Naa50 complex | - |
Schizosaccharomyces pombe |
| NatA/Naa50 complex | - |
Homo sapiens |
| NatA/Naa50 complex | - |
Saccharomyces cerevisiae |
| NatE | - |
Schizosaccharomyces pombe |
| NatE | - |
Homo sapiens |
| NatE | - |
Saccharomyces cerevisiae |
| ScNaa50 | - |
Saccharomyces cerevisiae |
| ScNatA | - |
Saccharomyces cerevisiae |
| SpNaa50 | - |
Schizosaccharomyces pombe |
| SpNatA | - |
Schizosaccharomyces pombe |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Schizosaccharomyces pombe |
| 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 | Homo sapiens |
| 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 | Saccharomyces cerevisiae |
| malfunction | yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association | Schizosaccharomyces pombe |
| malfunction | yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association | Homo sapiens |
| 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 | Saccharomyces cerevisiae |
| 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 | Schizosaccharomyces pombe |
| 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 | Homo sapiens |
| 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 | Saccharomyces cerevisiae |
| 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 | Schizosaccharomyces pombe |
| 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 | Homo sapiens |
| 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 | Saccharomyces cerevisiae |
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