Biology:N-alpha-acetyltransferase 10

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

N-alpha-acetyltransferase 10 (NAA10) also known as NatA catalytic subunit Naa10 and arrest-defective protein 1 homolog A (ARD1A) is an enzyme subunit that in humans is encoded NAA10 gene.[1][2] Together with its auxiliary subunit Naa15, Naa10 constitutes the NatA (Nα-acetyltransferase A) complex that specifically catalyzes the transfer of an acetyl group from acetyl-CoA to the N-terminal primary amino group of certain proteins. In higher eukaryotes, 5 other N-acetyltransferase (NAT) complexes, NatB-NatF, have been described that differ both in substrate specificity and subunit composition.[3]

Gene and transcripts

The human NAA10 is located on chromosome Xq28 and contains 8 exons, 2 encoding three different isoforms derived from alternate splicing.[4] Additionally, a processed NAA10 gene duplication NAA11 (ARD2) has been identified that is expressed in several human cell lines;[5] however, later studies indicate that Naa11 is not expressed in the human cell lines HeLa and HEK293 or in cancerous tissues, and NAA11 transcripts were only detected in testicular and placental tissues.[6] Naa11 has also been found in mouse, where it is mainly expressed in the testis.[7] NAA11 is located on chromosome 4q21.21 in human and 5 E3 in mouse, and only contains two exons. Mice have another Naa10-like paralog, Naa12. Naa12 has NAT activity and genetically compensates for loss of Naa10, while being Naa10/Naa12 null is embryonic lethal in mic.[8]

In mouse, NAA10 is located on chromosome X A7.3 and contains 9 exons. Two alternative splicing products of mouse Naa10, mNaa10235 and mNaa10225, were reported in NIH-3T3 and JB6 cells that may have different activities and function in different subcellular compartments.[9]

Homologues for Naa10 have been identified in almost all kingdoms of life analyzed, including plants,[10][11][12] fungi,[10][13] amoebozoa,[10] archaeabacteria[10][14][15][16] and protozoa.[17][18] In eubacteria, 3 Nα-acetyltransferases, RimI, RimJ and RimL, have been identified[19][20][21] but according to their low sequence identity with the NATs, it is likely that the RIM proteins do not have a common ancestor and evolved independently.[22][23]

Structure

Size-exclusion chromatography and circular dichroism indicated that human Naa10 consists of a compact globular region comprising two thirds of the protein and a flexible unstructured C-terminus.[24] X-ray crystal structure of the 100 kD holo-NatA (Naa10/Naa15) complex from S. pombe showed that Naa10 adopts a typical GNAT fold containing a N-terminal α1–loop–α2 segment that features one large hydrophobic interface and exhibits interactions with its auxiliary subunit Naa15, a central acetyl CoA-binding region, and C-terminal segments that are similar to the corresponding regions in Naa50, another Nα-acetyltransferase.[25] The X-ray crystal structure of archaeal T. volcanium Naa10 has also been reported, revealing multiple distinct modes of acetyl-Co binding involving the loops between β4 and α3, including the P-loop.[16] Non-complexed (Naa15 unbound) Naa10 adopts a different fold: Leu22 and Tyr26 shift out of the active site of Naa10, and Glu24 (important for substrate binding and catalysis of NatA) is repositioned by ~5 Å, resulting in a conformation that allows for the acetylation of a different subset of substrates.[25] An X-ray crystal structure of human Naa10 in complex with Naa15 and HYPK has been reported.[26]

A functional nuclear localization signal in the C-terminus of hNaa10 between residues 78 and 83 (KRSHRR) has been described.[27][28]

Function

Naa10, as part of the NatA complex, is bound to the ribosome and co-translationally acetylates proteins starting with small side chains such as Ser, Ala, Thr, Gly, Val and Cys, after the initiator methionine (iMet) has been cleaved by methionine aminopeptidases (MetAP).[29] Furthermore, post-translational acetylation by non-ribosome-associated Naa10 might occur. About 40-50 % of all proteins are potential NatA substrates.[3][30] Additionally, in a monomeric state, structural rearrangements of the substrate binding pocket Naa10 allow acetylation of N-termini with acidic side chains.[25][31] Furthermore, Nε-acetyltransferase activity[32][33][34][35][36][37][38] and N-terminal propionyltransferase activity [39] have been reported.

Despite the fact that Nα-terminal acetylation of proteins has been known for many years, the functional consequences of this modification are not well understood. However, accumulating evidence have linked Naa10 to various signaling pathways, including Wnt/β-catenin,[34][35][40][41] MAPK,[40] JAK/STAT,[42] and NF-κB,[43][44][45][46] thereby regulating various cellular processes, including cell migration,[47][48] cell cycle control,[49][50][51] DNA damage control,[45][52] caspase-dependent cell death,[52][53] p53 dependent apoptosis,[50] cell proliferation and autophagy [54] as well as hypoxia,[35][36][38][55][56] although there are some major discrepancies regarding hypoxia[57][58][59][60][61] and even isoform specific effects of Naa10 functions have been reported in mouse.[9][62]

Naa10 is essential in D. melanogaster,[63] C. elegans[64] and T. brucei.[17] In S. cerevisiae, Naa10 function is not essential but yNAA10Δ cells display severe defects including de-repression of the silent mating type locus (HML), failure to enter Go phase, temperature sensitivity, and impaired growth.[13][65] Naa10-knockout mice have very recently been reported to be viable, displaying a defect in bone development.[46]

Disease

In 2001 A c.109T>C (p.Ser37Pro) variant in NAA10 was identified in two unrelated families with Ogden Syndrome, a X-linked disorder involving a distinct combination of an aged appearance, craniofacial anomalies, hypotonia, global developmental delays, cryptorchidism, and cardiac arrhythmias.[66] Patient fibroblasts displayed altered morphology, growth and migration characteristics and molecular studies indicate that this S37P mutation disrupts the NatA complex and decreases Naa10 enzymatic activity in vitro and in vivo.[66][67][68]

Furthermore, two other mutations in Naa10 (R116W mutation in a boy and a V107F mutation in a girl) have been described in two unrelated families with sporadic cases of non-syndromic intellectual disabilities, postnatal growth failure, and skeletal anomalies.[69][70] The girl was reported as having delayed closure of the fontanels, delayed bone age, broad great toes, mild pectus carinatum, pulmonary artery stenosis, atrial septal defect, prolonged QT interval. The boy was reported as having small hands/feet, high arched palate, and wide interdental spaces.

Additionally, a splice mutation in the intron 7 splice donor site (c.471+2T→A) of NAA10 was reported in a single family with Lenz microphthalmia syndrome (LMS), a very rare, genetically heterogeneous X-linked recessive disorder characterized by microphthalmia or anophthalmia, developmental delay, intellectual disability, skeletal abnormalities and malformations of teeth, fingers and toes.[71] Patient fibroblasts displayed cell proliferation defects, dysregulation of genes involved in retinoic acid signaling pathway, such as STRA6, and deficiencies in retinol uptake.[71]

Accumulating evidence suggests Naa10 function might regulate co-translational protein folding through the modulation of chaperone function, thereby affecting pathological formation of toxic amyloid aggregates in Alzheimer's disease or prion [PSI+] propagation in yeast.[72][73][74][75]

Further information on NAA10 related syndromes can be found at www.naa10gene.com

Notes

References

  1. ↑ "Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae". Hum Mol Genet 3 (7): 1061–7. Jan 1995. doi:10.1093/hmg/3.7.1061. PMID 7981673. 
  2. ↑ "Entrez Gene: ARD1A ARD1 homolog A, N-acetyltransferase (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8260. 
  3. ↑ 3.0 3.1 "Protein N-terminal acetyltransferases: when the start matters". Trends in Biochemical Sciences 37 (4): 152–61. April 2012. doi:10.1016/j.tibs.2012.02.003. PMID 22405572. 
  4. ↑ "NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins". Nucleic Acids Research 35 (Database issue): D61–5. January 2007. doi:10.1093/nar/gkl842. PMID 17130148. 
  5. ↑ "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferase". BMC Biochemistry 7: 13. 25 April 2006. doi:10.1186/1471-2091-7-13. PMID 16638120. 
  6. ↑ "Expression of human NAA11 (ARD1B) gene is tissue-specific and is regulated by DNA methylation". Epigenetics 6 (11): 1391–9. November 2011. doi:10.4161/epi.6.11.18125. PMID 22048246. 
  7. ↑ "Cloning, characterization, and expression analysis of the novel acetyltransferase retrogene Ard1b in the mouse". Biology of Reproduction 81 (2): 302–9. August 2009. doi:10.1095/biolreprod.108.073221. PMID 19246321. 
  8. ↑ "Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway". eLife 10: e65952. August 2021. doi:10.7554/elife.65952. PMID 34355692. 
  9. ↑ 9.0 9.1 "Differential regulation of splicing, localization and stability of mammalian ARD1235 and ARD1225 isoforms". Biochemical and Biophysical Research Communications 353 (1): 18–25. 2 February 2007. doi:10.1016/j.bbrc.2006.11.131. PMID 17161380. 
  10. ↑ 10.0 10.1 10.2 10.3 "N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins". Journal of Molecular Biology 325 (4): 595–622. 24 January 2003. doi:10.1016/s0022-2836(02)01269-x. PMID 12507466. 
  11. ↑ "Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes". PLOS ONE 8 (3): e58681. 2013. doi:10.1371/journal.pone.0058681. PMID 23536812. Bibcode: 2013PLoSO...858681L. 
  12. ↑ "Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features". Molecular & Cellular Proteomics 11 (6): M111.015131. June 2012. doi:10.1074/mcp.m111.015131. PMID 22223895. 
  13. ↑ 13.0 13.1 "The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways". Cell 43 (2 Pt 1): 483–92. December 1985. doi:10.1016/0092-8674(85)90178-3. PMID 3907857. 
  14. ↑ "An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus". Molecular Microbiology 64 (6): 1540–8. June 2007. doi:10.1111/j.1365-2958.2007.05752.x. PMID 17511810. 
  15. ↑ "Expression, crystallization and preliminary X-ray crystallographic analyses of two N-terminal acetyltransferase-related proteins from Thermoplasma acidophilum". Acta Crystallographica Section F 62 (Pt 11): 1127–30. 1 November 2006. doi:10.1107/s1744309106040267. PMID 17077495. 
  16. ↑ 16.0 16.1 "Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1844 (10): 1790–7. October 2014. doi:10.1016/j.bbapap.2014.07.011. PMID 25062911. 
  17. ↑ 17.0 17.1 "Genetic manipulation indicates that ARD1 is an essential N(alpha)-acetyltransferase in Trypanosoma brucei". Molecular and Biochemical Parasitology 111 (2): 309–17. December 2000. doi:10.1016/s0166-6851(00)00322-4. PMID 11163439. 
  18. ↑ "N-terminal processing of proteins exported by malaria parasites". Molecular and Biochemical Parasitology 160 (2): 107–15. August 2008. doi:10.1016/j.molbiopara.2008.04.011. PMID 18534695. 
  19. ↑ "Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18". Molecular & General Genetics 177 (4): 645–51. 1980. doi:10.1007/bf00272675. PMID 6991870. 
  20. ↑ "Ribosomal protein modification in Escherichia coli. I. A mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity". Journal of Molecular Biology 131 (2): 169–89. 25 June 1979. doi:10.1016/0022-2836(79)90072-X. PMID 385889. 
  21. ↑ "Ribosomal protein modification in Escherichia coli. III. Studies of mutants lacking an acetylase activity specific for protein L12". Molecular & General Genetics 183 (3): 473–7. 1981. doi:10.1007/bf00268767. PMID 7038378. 
  22. ↑ "Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18". Protein Science 17 (10): 1781–90. October 2008. doi:10.1110/ps.035899.108. PMID 18596200. 
  23. ↑ "Composition and function of the eukaryotic N-terminal acetyltransferase subunits". Biochemical and Biophysical Research Communications 308 (1): 1–11. 15 August 2003. doi:10.1016/s0006-291x(03)01316-0. PMID 12890471. 
  24. ↑ "Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1". Protein Science 15 (8): 1968–76. August 2006. doi:10.1110/ps.062264006. PMID 16823041. 
  25. ↑ 25.0 25.1 25.2 "Molecular basis for N-terminal acetylation by the heterodimeric NatA complex". Nature Structural & Molecular Biology 20 (9): 1098–105. September 2013. doi:10.1038/nsmb.2636. PMID 23912279. 
  26. ↑ Gottlieb, Leah; Marmorstein, Ronen (10 May 2018). "Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK.". Structure 26 (7): 925–935.e8. doi:10.1016/j.str.2018.04.003. PMID 29754825. 
  27. ↑ "Identification and characterization of the human ARD1-NATH protein acetyltransferase complex". The Biochemical Journal 386 (Pt 3): 433–43. 15 March 2005. doi:10.1042/bj20041071. PMID 15496142. 
  28. ↑ "Nuclear translocation of hARD1 contributes to proper cell cycle progression". PLOS ONE 9 (8): e105185. 2014. doi:10.1371/journal.pone.0105185. PMID 25133627. Bibcode: 2014PLoSO...9j5185P. 
  29. ↑ "A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)". BMC Biochemistry 10: 15. 29 May 2009. doi:10.1186/1471-2091-10-15. PMID 19480662. 
  30. ↑ "NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation". PLOS Genetics 7 (7): e1002169. July 2011. doi:10.1371/journal.pgen.1002169. PMID 21750686. 
  31. ↑ "Proteome-derived peptide libraries allow detailed analysis of the substrate specificities of N(alpha)-acetyltransferases and point to hNaa10p as the post-translational actin N(alpha)-acetyltransferase". Molecular & Cellular Proteomics 10 (5): M110.004580. May 2011. doi:10.1074/mcp.m110.004580. PMID 21383206. 
  32. ↑ "Berberine inhibits HIF-1alpha expression via enhanced proteolysis". Molecular Pharmacology 66 (3): 612–9. September 2004. PMID 15322253. https://molpharm.aspetjournals.org/content/66/3/612/tab-article-info. 
  33. ↑ "Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A". Cell Death & Disease 5 (10): e1490. 23 October 2014. doi:10.1038/cddis.2014.456. PMID 25341044. 
  34. ↑ 34.0 34.1 "Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation". Cancer Research 66 (22): 10677–82. 15 November 2006. doi:10.1158/0008-5472.can-06-3171. PMID 17108104. 
  35. ↑ 35.0 35.1 35.2 "Hypoxia-inducible factor-1alpha obstructs a Wnt signaling pathway by inhibiting the hARD1-mediated activation of beta-catenin". Cancer Research 68 (13): 5177–84. 1 July 2008. doi:10.1158/0008-5472.can-07-6234. PMID 18593917. 
  36. ↑ 36.0 36.1 "Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation". Cell 111 (5): 709–20. 27 November 2002. doi:10.1016/S0092-8674(02)01085-1. PMID 12464182. 
  37. ↑ "Roles of arrest-defective protein 1(225) and hypoxia-inducible factor 1alpha in tumor growth and metastasis". Journal of the National Cancer Institute 102 (6): 426–42. 17 March 2010. doi:10.1093/jnci/djq026. PMID 20194889. 
  38. ↑ 38.0 38.1 "Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1". The EMBO Journal 25 (6): 1231–41. 22 March 2006. doi:10.1038/sj.emboj.7601025. PMID 16511565. 
  39. ↑ "Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo". Molecular & Cellular Proteomics 12 (1): 42–54. January 2013. doi:10.1074/mcp.m112.019299. PMID 23043182. 
  40. ↑ 40.0 40.1 "Arrest defective 1 autoacetylation is a critical step in its ability to stimulate cancer cell proliferation". Cancer Research 70 (11): 4422–32. 1 June 2010. doi:10.1158/0008-5472.can-09-3258. PMID 20501853. 
  41. ↑ "hNaa10p contributes to tumorigenesis by facilitating DNMT1-mediated tumor suppressor gene silencing". The Journal of Clinical Investigation 120 (8): 2920–30. August 2010. doi:10.1172/jci42275. PMID 20592467. 
  42. ↑ "Inhibition of STAT5a by Naa10p contributes to decreased breast cancer metastasis". Carcinogenesis 35 (10): 2244–53. October 2014. doi:10.1093/carcin/bgu132. PMID 24925029. 
  43. ↑ "Phosphorylation of ARD1 by IKKbeta contributes to its destabilization and degradation". Biochemical and Biophysical Research Communications 389 (1): 156–61. 6 November 2009. doi:10.1016/j.bbrc.2009.08.127. PMID 19716809. 
  44. ↑ "ARD1 binding to RIP1 mediates doxorubicin-induced NF-κB activation". Biochemical and Biophysical Research Communications 422 (2): 291–7. 1 June 2012. doi:10.1016/j.bbrc.2012.04.150. PMID 22580278. 
  45. ↑ 45.0 45.1 "N-α-acetyltransferase 10 protein inhibits apoptosis through RelA/p65-regulated MCL1 expression". Carcinogenesis 33 (6): 1193–202. June 2012. doi:10.1093/carcin/bgs144. PMID 22496479. 
  46. ↑ 46.0 46.1 "NAA10 controls osteoblast differentiation and bone formation as a feedback regulator of Runx2". Nature Communications 5: 5176. 7 November 2014. doi:10.1038/ncomms6176. PMID 25376646. Bibcode: 2014NatCo...5.5176Y. 
  47. ↑ "N-α-acetyltransferase 10 protein suppresses cancer cell metastasis by binding PIX proteins and inhibiting Cdc42/Rac1 activity". Cancer Cell 19 (2): 218–31. 15 February 2011. doi:10.1016/j.ccr.2010.11.010. PMID 21295525. 
  48. ↑ "Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase". PLOS ONE 4 (10): e7451. 14 October 2009. doi:10.1371/journal.pone.0007451. PMID 19826488. Bibcode: 2009PLoSO...4.7451S. 
  49. ↑ "Interaction between beta-catenin and HIF-1 promotes cellular adaptation to hypoxia". Nature Cell Biology 9 (2): 210–7. February 2007. doi:10.1038/ncb1534. PMID 17220880. 
  50. ↑ 50.0 50.1 "Depletion of the human Nα-terminal acetyltransferase A induces p53-dependent apoptosis and p53-independent growth inhibition". International Journal of Cancer 127 (12): 2777–89. 15 December 2010. doi:10.1002/ijc.25275. PMID 21351257. 
  51. ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 20 October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R. 
  52. ↑ 52.0 52.1 "A genome-wide RNAi screen reveals multiple regulators of caspase activation". The Journal of Cell Biology 179 (4): 619–26. 19 November 2007. doi:10.1083/jcb.200708090. PMID 17998402. 
  53. ↑ "Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival". Cell 146 (4): 607–20. 19 August 2011. doi:10.1016/j.cell.2011.06.050. PMID 21854985. 
  54. ↑ "ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR signaling pathway". Science Signaling 3 (108): ra9. 9 February 2010. doi:10.1126/scisignal.2000590. PMID 20145209. 
  55. ↑ "Down-regulation of the expression of the FIH-1 and ARD-1 genes at the transcriptional level by nickel and cobalt in the human lung adenocarcinoma A549 cell line". International Journal of Environmental Research and Public Health 2 (1): 10–3. April 2005. doi:10.3390/ijerph2005010010. PMID 16705796. 
  56. ↑ "Effect of connective tissue growth factor on hypoxia-inducible factor 1alpha degradation and tumor angiogenesis". Journal of the National Cancer Institute 98 (14): 984–95. 19 July 2006. doi:10.1093/jnci/djj242. PMID 16849681. 
  57. ↑ "Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha". FEBS Letters 579 (28): 6428–32. 21 November 2005. doi:10.1016/j.febslet.2005.10.036. PMID 16288748. 
  58. ↑ "Analysis of ARD1 function in hypoxia response using retroviral RNA interference". The Journal of Biological Chemistry 280 (18): 17749–57. 6 May 2005. doi:10.1074/jbc.m412055200. PMID 15755738. 
  59. ↑ "Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1alpha and is not induced by hypoxia or HIF". The Journal of Biological Chemistry 280 (35): 31132–40. 2 September 2005. doi:10.1074/jbc.m504482200. PMID 15994306. 
  60. ↑ "Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha". The Journal of Biological Chemistry 281 (19): 13612–9. 12 May 2006. doi:10.1074/jbc.m600456200. PMID 16543236. 
  61. ↑ "Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro". FEBS Letters 580 (8): 1911–8. 3 April 2006. doi:10.1016/j.febslet.2006.02.012. PMID 16500650. 
  62. ↑ "Characterization of ARD1 variants in mammalian cells". Biochemical and Biophysical Research Communications 340 (2): 422–7. 10 February 2006. doi:10.1016/j.bbrc.2005.12.018. PMID 16376303. 
  63. ↑ "Drosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complex". Developmental Dynamics 239 (11): 2813–27. November 2010. doi:10.1002/dvdy.22418. PMID 20882681. 
  64. ↑ "daf-31 encodes the catalytic subunit of N alpha-acetyltransferase that regulates Caenorhabditis elegans development, metabolism and adult lifespan". PLOS Genetics 10 (10): e1004699. October 2014. doi:10.1371/journal.pgen.1004699. PMID 25330189. 
  65. ↑ "The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus". Molecular and Cellular Biology 7 (10): 3713–22. October 1987. doi:10.1128/MCB.7.10.3713. PMID 3316986. 
  66. ↑ 66.0 66.1 "Using VAAST to identify an X-linked disorder resulting in lethality in male infants due to N-terminal acetyltransferase deficiency". American Journal of Human Genetics 89 (1): 28–43. 15 July 2011. doi:10.1016/j.ajhg.2011.05.017. PMID 21700266. 
  67. ↑ "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects". Human Molecular Genetics 24 (7): 1956–76. 8 December 2014. doi:10.1093/hmg/ddu611. PMID 25489052. 
  68. ↑ "A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase NAA10 Ser37Pro mutant". Molecular & Cellular Proteomics 13 (8): 2031–41. August 2014. doi:10.1074/mcp.m113.035402. PMID 24408909. 
  69. ↑ "Range of genetic mutations associated with severe non-syndromic sporadic intellectual disability: an exome sequencing study". Lancet 380 (9854): 1674–82. 10 November 2012. doi:10.1016/s0140-6736(12)61480-9. PMID 23020937. https://zenodo.org/record/3423600. 
  70. ↑ "De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females". European Journal of Human Genetics 23 (5): 602–609. 6 August 2014. doi:10.1038/ejhg.2014.150. PMID 25099252. 
  71. ↑ 71.0 71.1 "A splice donor mutation in NAA10 results in the dysregulation of the retinoic acid signalling pathway and causes Lenz microphthalmia syndrome". Journal of Medical Genetics 51 (3): 185–96. March 2014. doi:10.1136/jmedgenet-2013-101660. PMID 24431331. 
  72. ↑ "Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion". Journal of Biochemistry 137 (2): 147–55. February 2005. doi:10.1093/jb/mvi014. PMID 15749829. 
  73. ↑ "The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+ phenotype"]. Molecular Biology of the Cell 20 (3): 1068–80. February 2009. doi:10.1091/mbc.e08-04-0436. PMID 19073888. 
  74. ↑ "Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype". Nature Communications 5: 4384. 15 July 2014. doi:10.1038/ncomms5384. PMID 25023996. Bibcode: 2014NatCo...5.4384P. 
  75. ↑ "Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding". Nature Communications 5: 4383. 15 July 2014. doi:10.1038/ncomms5383. PMID 25023910. Bibcode: 2014NatCo...5.4383H. 

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: P41227 (N-alpha-acetyltransferase 10) at the PDBe-KB.



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