Towards a functional understanding of protein N-terminal acetylation

PLoS Biology

Volumn 9, Issue 5, 2011, Pages

  Arnesen, Thomas ^a,b  

^a UNIVERSITY OF BERGEN   (Norway)

^b HAUKELAND UNIVERSITY HOSPITAL   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; HISTONE H3; N TERMINAL ACYLTRANSFERASE; UNCLASSIFIED DRUG; PROTEIN;

ACETYLATION; AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENDOPLASMIC RETICULUM; FUNCTIONAL PROTEOMICS; HISTONE ACETYLATION; HUMAN; N TERMINAL ACETYLATION; NONHUMAN; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TARGETING; PROTEIN TRANSPORT; REGULATORY MECHANISM; GENETICS; METABOLISM; SECRETORY PATHWAY; SIGNAL TRANSDUCTION;

EUKARYOTA;

ACETYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; PROTEINS; SECRETORY PATHWAY; SIGNAL TRANSDUCTION;

EID: 79958039807     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001074     Document Type: Article

References (44)

1. Arnesen T, Van Damme P, Polevoda B, Helsens K, Evjenth R, et al. (2009) Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc Natl Acad Sci U S A 106: 8157-8162.
2. Brown J. L, Roberts W. K, (1976) Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nalpha-acetylated. J Biol Chem 251: 1009-1014.
3. NARITA K, (1958) Isolation of acetylpeptide from enzymic digests of TMV-protein. Biochim Biophys Acta 28: 184-191.
4. Gautschi M, Just S, Mun A, Ross S, Rücknagel P, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23: 7403-7414.
5. Pestana A, Pitot H. C, (1975) Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro. Biochemistry 14: 1404-1412.
6. Polevoda B, Brown S, Cardillo T. S, Rigby S, Sherman F, (2008) Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes. J Cell Biochem 103: 492-508.
7. Strous G. J, Berns A. J, Bloemendal H, (1974) N-terminal acetylation of the nascent chains of alpha-crystallin. Biochem Biophys Res Commun 58: 876-884.
8. Polevoda B, Arnesen T, Sherman F, (2009) A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proc 3 (Suppl 6): S2.
9. Goetze S, Qeli E, Mosimann C, Staes A, Gerrits B, et al. (2009) Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster. PLoS Biol 7: e1000236 doi:10.1371/journal.pbio.1000236.
10. Polevoda B, Norbeck J, Takakura H, Blomberg A, Sherman F, (1999) Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae. EMBO J 18: 6155-6168.
11. Jornvall H, (1975) Acetylation of protein N-terminal amino groups structural observations on alpha-amino acetylated proteins. J Theor Biol 55: 1-12.
12. Persson B, Flinta C, von Heijne G, Jornvall H, (1985) Structures of N-terminally acetylated proteins. Eur J Biochem 152: 523-527.
13. Hershko A, Heller H, Eytan E, Kaklij G, Rose I. A, (1984) Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown. Proc Natl Acad Sci U S A 81: 7021-7025.
14. Ben Saadon R, Fajerman I, Ziv T, Hellman U, Schwartz A. L, et al. (2004) The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue. J Biol Chem 279: 41414-41421.
15. Ciechanover A, Ben Saadon R, (2004) N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol 14: 103-106.
16. Kuo M. L, den Besten W, Bertwistle D, Roussel M. F, Sherr C. J, (2004) N-terminal polyubiquitination and degradation of the Arf tumor suppressor. Genes Dev 18: 1862-1874.
17. Pena M. M, Melo S. P, Xing Y. Y, White K, Barbour K. W, et al. (2009) The intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathway. J Biol Chem 284: 31597-31607.
18. Hwang C. S, Shemorry A, Varshavsky A, (2010) N-terminal acetylation of cellular proteins creates specific degradation signals. Science 327: 973-977.
19. Varshavsky A, (2008) Discovery of cellular regulation by protein degradation. J Biol Chem 283: 34469-34489.
20. Helbig A. O, Rosati S, Pijnappel P. W, van Breukelen B, Timmers M. H, et al. (2010) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics 11: 685.
21. Coulton A. T, East D. A, Galinska-Rakoczy A, Lehman W, Mulvihill D. P, (2010) The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast. J Cell Sci 123: 3235-3243.
22. Polevoda B, Cardillo T. S, Doyle T. C, Bedi G. S, Sherman F, (2003) Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin. J Biol Chem 278: 30686-30697.
23. Singer J. M, Shaw J. M, (2003) Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast. Proc Natl Acad Sci U S A 100: 7644-7649.
24. Caesar R, Blomberg A, (2004) The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway. J Biol Chem 279: 38532-38543.
25. Behnia R, Panic B, Whyte J. R, Munro S, (2004) Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. Nat Cell Biol 6: 405-413.
26. Behnia R, Barr F. A, Flanagan J. J, Barlowe C, Munro S, (2007) The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic. J Cell Biol 176: 255-261.
27. Setty S. R, Strochlic T. I, Tong A. H, Boone C, Burd C. G, (2004) Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation and the integral membrane protein Sys1p. Nat Cell Biol 6: 414-419.
28. Murthi A, Hopper A. K, (2005) Genome-wide screen for inner nuclear membrane protein targeting in Saccharomyces cerevisiae: roles for N-acetylation and an integral membrane protein. Genetics 170: 1553-1560.
29. Caesar R, Warringer J, Blomberg A, (2006) Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB. Eukaryot Cell 5: 368-378.
30. Geissenhoner A, Weise C, Ehrenhofer-Murray A. E, (2004) Dependence of ORC silencing function on NatA-mediated Nalpha acetylation in Saccharomyces cerevisiae. Mol Cell Biol 24: 10300-10312.
31. Wang X, Connelly J. J, Wang C. L, Sternglanz R, (2004) Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing. Genetics 168: 547-551.
32. van Welsem T, Frederiks F, Verzijlbergen K. F, Faber A. W, Nelson Z. W, et al. (2008) Synthetic lethal screens identify gene silencing processes in yeast and implicate the acetylated amino terminus of Sir3 in recognition of the nucleosome core. Mol Cell Biol 28: 3861-3872.
33. Forte G. M. A, Pool M. R, Stirling C. J, (2011) N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol 9: e1001073 doi:10.1371/journal.pbio.1001073.
34. Martoglio B, Dobberstein B, (1998) Signal sequences: more than just greasy peptides. Trends Cell Biol 8: 410-415.
35. Ng D. T, Brown J. D, Walter P, (1996) Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 134: 269-278.
36. Becker T, Bhushan S, Jarasch A, Armache J. P, Funes S, et al. (2009) Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome. Science 326: 1369-1373.
37. Halic M, Beckmann R, (2005) The signal recognition particle and its interactions during protein targeting. Curr Opin Struct Biol 15: 116-125.
38. Kalies K. U, Gorlich D, Rapoport T. A, (1994) Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J Cell Biol 126: 925-934.
39. Shan S. O, Walter P, (2005) Co-translational protein targeting by the signal recognition particle. FEBS Lett 579: 921-926.
40. Chirico W. J, Waters M. G, Blobel G, (1988) 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332: 805-810.
41. Deshaies R. J, Koch B. D, Werner-Washburne M, Craig E. A, Schekman R, (1988) A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800-805.
42. Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport T. A, (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81: 561-570.
43. Plath K, Rapoport T. A, (2000) Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum. J Cell Biol 151: 167-178.
44. Berndt U, Oellerer S, Zhang Y, Johnson A. E, Rospert S, (2009) A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel. Proc Natl Acad Sci U S A 106: 1398-1403.