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词条 N-alpha-acetyltransferase 10
释义

  1. Gene and transcripts

  2. Structure

  3. Function

  4. Disease

  5. Notes

  6. References

  7. Further reading

{{Infobox gene}}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.

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.[8]

Homologues for Naa10 have been identified in almost all kingdoms of life analyzed, including plants,[9][10][11] fungi,[9][12] amoebozoa,[9] archaeabacteria[9][13][14][15] and protozoa.[16][17] In eubacteria, 3 Nα-acetyltransferases, RimI, RimJ and RimL, have been identified[18][19][20] 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.[21][22]

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.[23] 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.[24] 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.[15] 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.[24] An X-ray crystal structure of human Naa10 in complex with Naa15 and HYPK has been reported.[25]

A functional nuclear localization signal in the C-terminus of hNaa10 between residues 78 and 83 (KRSHRR) has been described.[26][27]

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).[28] Furthermore, post-translational acetylation by non-ribosome-associated Naa10 might occur. About 40-50 % of all proteins are potential NatA substrates.[3][29] Additionally, in a monomeric state, structural rearrangements of the substrate binding pocket Naa10 allow acetylation of N-termini with acidic side chains.[24][30] Furthermore, Nε-acetyltransferase activity[31][32][33][34][35][36][37] and N-terminal propionyltransferase activity [38] 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,[33][34][39][40] MAPK,[39] JAK/STAT,[41] and NF-κB,[42][43][44][45] thereby regulating various cellular processes, including cell migration,[46][47] cell cycle control,[48][49][50] DNA damage control,[44][51] caspase-dependent cell death,[51][52] p53 dependent apoptosis,[49] cell proliferation and autophagy [53] as well as hypoxia,[34][35][37][54][55] although there are some major discrepancies regarding hypoxia[56][57][58][59][60] and even isoform specific effects of Naa10 functions have been reported in mouse.[8][61]

Naa10 is essential in D. melanogaster,[62] C. elegans[63] and T. brucei.[16] 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.[12][64] Naa10-knockout mice have very recently been reported to be viable, displaying a defect in bone development.[45]

Disease

Recently, 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.[65] 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.[65][66][67]

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.[68][69] 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.[70] Patient fibroblasts displayed cell proliferation defects, dysregulation of genes involved in retinoic acid signaling pathway, such as STRA6, and deficiencies in retinol uptake.[70]

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.[71][72][73][74]

Notes

{{Academic-written review
| wikidate = 2014
| journal = Gene
| title = {{#property:P1476|from=Q28638824}}
| authors = {{#property:P2093|from=Q28638824}}
| date = {{#property:P577|from=Q28638824}}
| volume = {{#property:P478|from=Q28638824}}
| issue = {{#property:P433|from=Q28638824}}
| pages = {{#property:P304|from=Q28638824}}
| doi = {{#property:P356|from=Q28638824}}
| pmid = {{#property:P698|from=Q28638824}}
| pmc = {{#property:P932|from=Q28638824}}
}}

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51. ^1 {{cite journal | vauthors = Yi CH, Sogah DK, Boyce M, Degterev A, Christofferson DE, Yuan J | title = A genome-wide RNAi screen reveals multiple regulators of caspase activation | journal = The Journal of Cell Biology | volume = 179 | issue = 4 | pages = 619–26 | date = 19 November 2007 | pmid = 17998402 | doi=10.1083/jcb.200708090 | pmc=2080898}}
52. ^{{cite journal | vauthors = Yi CH, Pan H, Seebacher J, Jang IH, Hyberts SG, Heffron GJ, Vander Heiden MG, Yang R, Li F, Locasale JW, Sharfi H, Zhai B, Rodriguez-Mias R, Luithardt H, Cantley LC, Daley GQ, Asara JM, Gygi SP, Wagner G, Liu CF, Yuan J | title = Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival | journal = Cell | volume = 146 | issue = 4 | pages = 607–20 | date = 19 August 2011 | pmid = 21854985 | doi=10.1016/j.cell.2011.06.050 | pmc=3182480}}
53. ^{{cite journal | vauthors = Kuo HP, Lee DF, Chen CT, Liu M, Chou CK, Lee HJ, Du Y, Xie X, Wei Y, Xia W, Weihua Z, Yang JY, Yen CJ, Huang TH, Tan M, Xing G, Zhao Y, Lin CH, Tsai SF, Fidler IJ, Hung MC | title = ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR signaling pathway | journal = Science Signaling | volume = 3 | issue = 108 | pages = ra9 | date = 9 February 2010 | pmid = 20145209 | doi=10.1126/scisignal.2000590 | pmc=2874891}}
54. ^{{cite journal | vauthors = Ke Q, Kluz T, Costa M | title = 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 | journal = International Journal of Environmental Research and Public Health | volume = 2 | issue = 1 | pages = 10–3 | date = April 2005 | pmid = 16705796 | doi=10.3390/ijerph2005010010 | pmc=3814691}}
55. ^{{cite journal | vauthors = Chang CC, Lin MT, Lin BR, Jeng YM, Chen ST, Chu CY, Chen RJ, Chang KJ, Yang PC, Kuo ML | title = Effect of connective tissue growth factor on hypoxia-inducible factor 1alpha degradation and tumor angiogenesis | journal = Journal of the National Cancer Institute | volume = 98 | issue = 14 | pages = 984–95 | date = 19 July 2006 | pmid = 16849681 | doi=10.1093/jnci/djj242}}
56. ^{{cite journal | vauthors = Arnesen T, Kong X, Evjenth R, Gromyko D, Varhaug JE, Lin Z, Sang N, Caro J, Lillehaug JR | title = Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha | journal = FEBS Letters | volume = 579 | issue = 28 | pages = 6428–32 | date = 21 November 2005 | pmid = 16288748 | doi=10.1016/j.febslet.2005.10.036| pmc = 4505811 }}
57. ^{{cite journal | vauthors = Fisher TS, Etages SD, Hayes L, Crimin K, Li B | title = Analysis of ARD1 function in hypoxia response using retroviral RNA interference | journal = The Journal of Biological Chemistry | volume = 280 | issue = 18 | pages = 17749–57 | date = 6 May 2005 | pmid = 15755738 | doi=10.1074/jbc.m412055200}}
58. ^{{cite journal | vauthors = Bilton R, Mazure N, Trottier E, Hattab M, Déry MA, Richard DE, Pouysségur J, Brahimi-Horn MC | title = Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1alpha and is not induced by hypoxia or HIF | journal = The Journal of Biological Chemistry | volume = 280 | issue = 35 | pages = 31132–40 | date = 2 September 2005 | pmid = 15994306 | doi=10.1074/jbc.m504482200}}
59. ^{{cite journal | vauthors = Fath DM, Kong X, Liang D, Lin Z, Chou A, Jiang Y, Fang J, Caro J, Sang N | title = Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha | journal = The Journal of Biological Chemistry | volume = 281 | issue = 19 | pages = 13612–9 | date = 12 May 2006 | pmid = 16543236 | doi=10.1074/jbc.m600456200 | pmc=1564196}}
60. ^{{cite journal | vauthors = Murray-Rust TA, Oldham NJ, Hewitson KS, Schofield CJ | title = Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro | journal = FEBS Letters | volume = 580 | issue = 8 | pages = 1911–8 | date = 3 April 2006 | pmid = 16500650 | doi=10.1016/j.febslet.2006.02.012}}
61. ^{{cite journal | vauthors = Kim SH, Park JA, Kim JH, Lee JW, Seo JH, Jung BK, Chun KH, Jeong JW, Bae MK, Kim KW | title = Characterization of ARD1 variants in mammalian cells | journal = Biochemical and Biophysical Research Communications | volume = 340 | issue = 2 | pages = 422–7 | date = 10 February 2006 | pmid = 16376303 | doi=10.1016/j.bbrc.2005.12.018}}
62. ^{{cite journal | vauthors = Wang Y, Mijares M, Gall MD, Turan T, Javier A, Bornemann DJ, Manage K, Warrior R | title = Drosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complex | journal = Developmental Dynamics | volume = 239 | issue = 11 | pages = 2813–27 | date = November 2010 | pmid = 20882681 | doi=10.1002/dvdy.22418 | pmc=3013298}}
63. ^{{cite journal | vauthors = Chen D, Zhang J, Minnerly J, Kaul T, Riddle DL, Jia K | title = daf-31 encodes the catalytic subunit of N alpha-acetyltransferase that regulates Caenorhabditis elegans development, metabolism and adult lifespan | journal = PLOS Genetics | volume = 10 | issue = 10 | pages = e1004699 | date = October 2014 | pmid = 25330189 | doi=10.1371/journal.pgen.1004699 | pmc=4199510}}
64. ^{{cite journal | vauthors = Whiteway M, Freedman R, Van Arsdell S, Szostak JW, Thorner J | title = The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus | journal = Molecular and Cellular Biology | volume = 7 | issue = 10 | pages = 3713–22 | date = October 1987 | pmid = 3316986 | pmc=368027| doi = 10.1128/MCB.7.10.3713 }}
65. ^1 {{cite journal | vauthors = Rope AF, Wang K, Evjenth R, Xing J, Johnston JJ, Swensen JJ, Johnson WE, Moore B, Huff CD, Bird LM, Carey JC, Opitz JM, Stevens CA, Jiang T, Schank C, Fain HD, Robison R, Dalley B, Chin S, South ST, Pysher TJ, Jorde LB, Hakonarson H, Lillehaug JR, Biesecker LG, Yandell M, Arnesen T, Lyon GJ | title = Using VAAST to identify an X-linked disorder resulting in lethality in male infants due to N-terminal acetyltransferase deficiency | journal = American Journal of Human Genetics | volume = 89 | issue = 1 | pages = 28–43 | date = 15 July 2011 | pmid = 21700266 | doi=10.1016/j.ajhg.2011.05.017 | pmc=3135802}}
66. ^{{cite journal | vauthors = Myklebust LM, Van Damme P, Støve SI, Dörfel MJ, Abboud A, Kalvik TV, Grauffel C, Jonckheere V, Wu Y, Swensen J, Kaasa H, Liszczak G, Marmorstein R, Reuter N, Lyon GJ, Gevaert K, Arnesen T | title = Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects | journal = Human Molecular Genetics | date = 8 December 2014 | pmid = 25489052 | doi=10.1093/hmg/ddu611 | volume=24 | issue = 7 | pages=1956–76 | pmc=4355026}}
67. ^{{cite journal | vauthors = Van Damme P, Støve SI, Glomnes N, Gevaert K, Arnesen T | title = A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase NAA10 Ser37Pro mutant | journal = Molecular & Cellular Proteomics | volume = 13 | issue = 8 | pages = 2031–41 | date = August 2014 | pmid = 24408909 | doi=10.1074/mcp.m113.035402 | pmc=4125735}}
68. ^{{cite journal | vauthors = Rauch A, Wieczorek D, Graf E, Wieland T, Endele S, Schwarzmayr T, Albrecht B, Bartholdi D, Beygo J, Di Donato N, Dufke A, Cremer K, Hempel M, Horn D, Hoyer J, Joset P, Röpke A, Moog U, Riess A, Thiel CT, Tzschach A, Wiesener A, Wohlleber E, Zweier C, Ekici AB, Zink AM, Rump A, Meisinger C, Grallert H, Sticht H, Schenck A, Engels H, Rappold G, Schröck E, Wieacker P, Riess O, Meitinger T, Reis A, Strom TM | title = Range of genetic mutations associated with severe non-syndromic sporadic intellectual disability: an exome sequencing study | journal = Lancet | volume = 380 | issue = 9854 | pages = 1674–82 | date = 10 November 2012 | pmid = 23020937 | doi=10.1016/s0140-6736(12)61480-9}}
69. ^{{cite journal | vauthors = Popp B, Støve SI, Endele S, Myklebust LM, Hoyer J, Sticht H, Azzarello-Burri S, Rauch A, Arnesen T, Reis A | title = De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females | journal = European Journal of Human Genetics | date = 6 August 2014 | pmid = 25099252 | doi=10.1038/ejhg.2014.150 | volume=23 | issue = 5 | pages=602–609 | pmc=4402627}}
70. ^1 {{cite journal | vauthors = Esmailpour T, Riazifar H, Liu L, Donkervoort S, Huang VH, Madaan S, Shoucri BM, Busch A, Wu J, Towbin A, Chadwick RB, Sequeira A, Vawter MP, Sun G, Johnston JJ, Biesecker LG, Kawaguchi R, Sun H, Kimonis V, Huang T | title = A splice donor mutation in NAA10 results in the dysregulation of the retinoic acid signalling pathway and causes Lenz microphthalmia syndrome | journal = Journal of Medical Genetics | volume = 51 | issue = 3 | pages = 185–96 | date = March 2014 | pmid = 24431331 | doi=10.1136/jmedgenet-2013-101660 | pmc=4278941}}
71. ^{{cite journal | vauthors = Asaumi M, Iijima K, Sumioka A, Iijima-Ando K, Kirino Y, Nakaya T, Suzuki T | title = Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion | journal = Journal of Biochemistry | volume = 137 | issue = 2 | pages = 147–55 | date = February 2005 | pmid = 15749829 | doi=10.1093/jb/mvi014}}
72. ^{{cite journal | vauthors = Pezza JA, Langseth SX, Raupp Yamamoto R, Doris SM, Ulin SP, Salomon AR, Serio TR | title = The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype | journal = Molecular Biology of the Cell | volume = 20 | issue = 3 | pages = 1068–80 | date = February 2009 | pmid = 19073888 | doi=10.1091/mbc.e08-04-0436 | pmc=2633373}}
73. ^{{cite journal | vauthors = Pezza JA, Villali J, Sindi SS, Serio TR | title = Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype | journal = Nature Communications | volume = 5 | pages = 4384 | date = 15 July 2014 | pmid = 25023996 | doi=10.1038/ncomms5384 | pmc=4156856}}
74. ^{{cite journal | vauthors = Holmes WM, Mannakee BK, Gutenkunst RN, Serio TR | title = Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding | journal = Nature Communications | volume = 5 | pages = 4383 | date = 15 July 2014 | pmid = 25023910 | doi=10.1038/ncomms5383 | pmc=4140192}}

Further reading

{{refbegin|35em}}
  • {{cite journal | vauthors = Brenner V, Nyakatura G, Rosenthal A, Platzer M | title = Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse | journal = Genomics | volume = 44 | issue = 1 | pages = 8–14 | year = 1997 | pmid = 9286695 | doi = 10.1006/geno.1997.4822 }}
  • {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Res. | volume = 10 | issue = 11 | pages = 1788–95 | year = 2001 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
  • {{cite journal | vauthors = Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S | title = Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing | journal = EMBO Rep. | volume = 1 | issue = 3 | pages = 287–92 | year = 2001 | pmid = 11256614 | pmc = 1083732 | doi = 10.1093/embo-reports/kvd058 }}
  • {{cite journal | vauthors = Sugiura N, Adams SM, Corriveau RA | title = An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development | journal = J. Biol. Chem. | volume = 278 | issue = 41 | pages = 40113–20 | year = 2003 | pmid = 12888564 | doi = 10.1074/jbc.M301218200 }}
  • {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Res. | volume = 14 | issue = 10B | pages = 2136–44 | year = 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
  • {{cite journal | vauthors = Arnesen T, Gromyko D, Horvli O, Fluge Ø, Lillehaug J, Varhaug JE | title = Expression of N-acetyl transferase human and human Arrest defective 1 proteins in thyroid neoplasms | journal = Thyroid | volume = 15 | issue = 10 | pages = 1131–6 | year = 2006 | pmid = 16279846 | doi = 10.1089/thy.2005.15.1131 }}
  • {{cite journal | vauthors = Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S | title = The LIFEdb database in 2006 | journal = Nucleic Acids Res. | volume = 34 | issue = Database issue | pages = D415–8 | year = 2006 | pmid = 16381901 | pmc = 1347501 | doi = 10.1093/nar/gkj139 }}
  • {{cite journal | vauthors = Arnesen T, Gromyko D, Pendino F, Ryningen A, Varhaug JE, Lillehaug JR | title = Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex | journal = Oncogene | volume = 25 | issue = 31 | pages = 4350–60 | year = 2006 | pmid = 16518407 | doi = 10.1038/sj.onc.1209469 }}
  • {{cite journal | vauthors = Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP | title = A probability-based approach for high-throughput protein phosphorylation analysis and site localization | journal = Nat. Biotechnol. | volume = 24 | issue = 10 | pages = 1285–92 | year = 2006 | pmid = 16964243 | doi = 10.1038/nbt1240 }}
{{refend}}{{Use dmy dates|date=April 2017}}

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