Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae

EMBO Journal

Volumn 18, Issue 21, 1999, Pages 6155-6168

  Polevoda, Bogdan ^a   Norbeck, Joakim ^b   Takakura, Hikaru ^c   Blomberg, Anders ^b   Sherman, Fred ^a  

^a UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

^b UNIVERSITY OF GOTHENBURG   (Sweden)

^c TAKARA SHUZO CO LTD   (Japan)

Author keywords

Acetylation; N terminal acetyltransferase; Protein modification; Saccharomyces cerevisiae

Indexed keywords

ACYLTRANSFERASE; FUNGAL PROTEIN; GLYCEROL; MUTANT PROTEIN; SODIUM CHLORIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; FUNGUS GROWTH; MATING; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

ACETYLATION; ACETYLTRANSFERASES; AMINO ACID SEQUENCE; BASE SEQUENCE; CYTOCHROME C GROUP; CYTOCHROMES C; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; FUNGAL PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PHENOTYPE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0033231015     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.21.6155     Document Type: Article

References (65)

1. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. and Lipman, D.J. (1990) Basic local alignment search tool. J. Mol. Biol., 215, 403-410.
2. Arendt, C.S. and Hochstrasser, M. (1999) Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J., 18, 3575-3585.
3. Arfin, S.M., Kendall, R.L., Hall, L., Weaver, L.H., Stewart, A.E., Matthews, B.W. and Bradshaw, R.A. (1995) Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl Acad. Sci. USA, 92, 7714-7718.
4. Augen, J. and Wold, F. (1986) How much sequence information is needed for the regulation of amino-terminal acetylation of eukaryotic proteins. Trends Biochem. Sci., 11, 494-497.
5. Baim, S.B., Pietras, D.F., Eustice, D.C. and Sherman, F. (1985) A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c. Mol. Cell. Biol., 5, 1839-1846.
6. 2 terminus and a prolyl substitution for the normal histidyl residue 2 of the b chain. Proc. Natl Acad. Sci. USA, 82, 4602-4605.
7. Baudin, A., Ozier, K.O., Denouel, A., Lacroute, F. and Cullin, C. (1993) A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae. Nucleic Acids Res., 21, 3329-3330.
8. Blomberg, A. et al. (1995) Interlaboratory reproducibility of yeast protein patterns analyzed by immobilized pH gradient two-dimensional gel electrophoresis. Electrophoresis, 16, 1935-1945.
9. Boucherie, H., Sagliocco, F., Joubert, R., Maillet, I., Labarre, J. and Perrot, M. (1996) Two-dimensional gel protein database of Saccharomyces cerevisiae. Electrophoresis, 17, 1683-1699.
10. α-acetyl transferase families. Trends Biochem. Sci., 23, 263-267.
11. Coleman, C.S., Huang, H. and Pegg, A.E. (1996) Structure and critical residues at the active site of spermidine/spermine-N1-acetyltransferase. Biochem. J., 316, 697-701.
12. Cook, R.K., Sheff, D.R. and Rubenstein, P.A. (1991) Unusual metabolism of the yeast actin amino terminus. J. Biol. Chem., 266, 16825-16833.
13. Corey, E.J., Matsuda, S.P.T. and Bartel, B. (1994) Molecular cloning, characterization and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase. Proc. Natl Acad. Sci. USA, 91, 2211-2215.
14. Corpet, F. (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res., 16, 10881-10890.
15. Dores, R.M., McDonald, L.K., Steveson, T.C. and Sei, C.A. (1990) The molecular evolution of neuropeptides: prospects for the '90s. Brain Behavior Evol., 36, 80-99.
16. Driessen, H.P.C., de Jong, W.W., Tesser, G.I. and Bloemendal, H. (1985) The mechanism of N-terminal acetylation of proteins. CRC Crit. Rev. Biochem., 18, 281-325.
17. Dutnall, R.N, Tafrov, S.T., Strenglanz, R. and Ramakrishnan, V. (1998) Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell, 94, 427-438.
18. +, a gene that interacts with mutations in the Arp2/3 complex and actin. Genetics, 152, 895-908.
19. Flinta, C., Persson, B., Jörnvall, H. and von Heijne, G. (1986) Sequence determinants of cytosolic N-terminal protein processing. Eur. J. Biochem., 154, 193-6.
20. Garrels, J.I. et al. (1997) Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins. Electrophoresis, 18, 1347-1360.
21. Glembotski, C.C. (1982a) Acetylation of α-melanotropin and β-endorphin in the rat intermediate pituitary. J. Biol. Chem., 257, 10493-10500.
22. Glembotski, C.C. (1982b) Characterization of the peptide acetyltransferase activity in bovine and rat intermediate pituitaries responsible for the acetylation of β-endorphin and α-melanotropin. J. Biol. Chem., 257, 10501-10509.
23. Hickman, A.B., Namboodiri, M.A.A., Klein, D.C. and Dyda, F. (1999) The structural basis of ordered substrate binding by serotonin N-acetyltransferase : enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell, 97, 361-369.
24. Hilfiker, A., Hilfiker-Kleiner, D., Pannuti, A. and Lucchesi, J.C. (1997) mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to SAS genes of yeast, is required for dosage compensation in Drosophila. EMBO J., 16, 2054-2060.
25. Huang, S. et al. (1987) Specificity of cotranslational amino-terminal processing of proteins in yeast. Biochemistry, 26, 8242-8246.
26. Jörnvall, H. (1975) Acetylation of protein N-terminal amino groups: structural observations on α-amino acetylated proteins. J. Theor. Biol., 55, 1-12.
27. Kendall, R.L., Yamada, R. and Bradshaw, R.A. (1990) Cotranslational amino-terminal process. Methods Enzymol., 185, 398-407.
28. α-acetyltransferase in the yeast Saccharomyces cerevisiae. J. Biol. Chem., 269, 13141-13147.
29. Kuo, M.H., Zhou, J., Jambeck, P., Churchill, M.E. and Allis, C.D. (1998) Histone acetyltransferase activity of yeast Gcn5 is required for the activation of target genes in vivo. Genes Dev., 12, 627-639.
30. α-acetyltransferase from Saccharomyces cerevisiae. J. Biol. Chem., 263, 14948-14955.
31. α-acetyltransferase from Saccharomyces cerevisiae. J. Biol. Chem., 264, 12339-12343.
32. α-acetylation is required for normal growth and mating of Saccharomyces cerevisiae. J. Bacteriol., 171, 5795-5802.
33. 2-terminal methionine residues: purification and partial characterization. Biochim. Biophys. Acta, 1338, 244-252.
34. Li, X. and Chang, Y.-H. (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl Acad. Sci. USA, 92, 12357-12361.
35. Lin, Y., Fletcher, C.M., Zhou, J., Allis, D and Wagner, G. (1999) Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Nature, 400, 86-89.
36. Moerschell, R.P., Hosokawa, Y., Tsunasawa, S. and Sherman, F. (1990) The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo: processing of altered iso-1-cytochromes c created by oligonucleotide transformation. J. Biol. Chem., 265, 19638-19643.
37. Mullen, J.R., Kayne, P.S., Moerschell, R.P., Tsunasawa, S., Gribskov, M., Colavito-Shepanski, M., Grunstein, M., Sherman, F. and Sternglanz, R. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J., 8, 2067-2075.
38. Neuwald, A.F. and Landsman, D. (1997) GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci., 22, 154-155.
39. Norbeck, J. and Blomberg, A. (1997) Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension: reproducibility and evidence for isoelectric focusing of alkaline proteins. Yeast, 13, 1519-1534.
40. Park, E.-C. and Szostak, J.W. (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J., 11, 2087-2093.
41. Persson, B., Flinta, C., von Heijne, G. and Jörnvall, H. (1985) Structures of N-terminally acetylated proteins. Eur. J. Biochem., 152, 523-527.
42. Prchal, J.T., Cashman, D.P. and Kan, Y.W. (1986) Hemoglobin Long Island is caused by a single mutation (adenine to cytosine) resulting in a failure to cleave amino-terminal methionine. Proc. Natl Acad. Sci. USA, 83, 24-27.
43. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
44. Schagger, H. and von Jagob, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
45. Sherman, F. (1991) Getting started with yeast. Methods Enzymol., 194, 3-21.
46. Sherman, F. and Slonimski, P.P. (1964) Respiration-deficient mutants of yeast. Biochim. Biophys. Acta, 90, 1-15.
47. Sherman, F., Stewart, J.W. and Tsunasawa, S. (1985) Methionine or not methionine at the beginning of a protein. BioEssays, 3, 27-31.
48. Sherman, F., Moerschell, R.P., Tsunasawa, S. and Sternglanz, R. (1993) N-terminal acetylation of mutationally altered form of iso-1-cytochromes c in normal and nat1 strains deficient in the major N-terminal acetyl transferase of the yeast Saccharomyces cerevisiae. In Imahori, K. and Sakiyama, F. (eds), Methods in Protein Sequence Analysis. Plenum, New York, NY, pp. 173-181.
49. Smith, E.R., Eisen, A., Gu, W., Sattah, M., Pannuti, A., Zhou, J., Cook, R.G., Lucchesi, J.C. and Allis, C.D. (1998) ESA1 is a histone acetyltransferase that is essential for growth in yeast. Proc. Natl Acad. Sci. USA, 95, 3561-3565.
50. Smith, T.F. and Waterman, M.S. (1981) Comparison of bio-sequences. Adv. Appl. Math., 2, 482-489.
51. Symth, D.G. and Zakarian, S. (1980) Selective processing of β-endorphin in regions of porcine pituitary. Nature, 288, 613-615.
52. Symth, D.G., Massey, D.E., Zakarian, S. and Finnie,. D.A. (1979) Endorphins are stored in biologically active and inactive forms: isolation of α-N-acetyl peptides. Nature, 279, 252-254.
53. 2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae. J. Biol. Chem., 267, 5442-5445.
54. 2 terminus is necessary for virus particle assembly. J. Biol. Chem., 267, 20277-20281.
55. Tercero, J.C, Riles, L.E. and Wickner, R.B. (1992) Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae. J. Biol. Chem., 267, 20270-20276.
56. Tercero, J.C., Dinman, J.D. and Wickner, R.B. (1993) Specificity of the yeast MAK3 N-acetyltransferase that modifies gag of the L-A dsRNA virus. J. Bacteriol., 175, 3192-3194.
57. Tribioli, C., Mancini, M., Plassart, E., Bione, S., Rivella, S., Sala, C., Torri, G. and Toniolo, D. (1994) Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyltransferase of Saccharomyces cerevisiae. Hum. Mol. Genet., 3, 1061-1067.
58. Tsunasawa, S., Stewart, J.W. and Sherman, F. (1985) Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c: the specificities of methionine aminopeptides and acetyltransferase. J. Biol. Chem., 260, 5382-5391.
59. Wach, A., Brachat, A., Pohlmann, R. and Philippsen, P. (1994) New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast, 10, 1793-1808.
60. Wang, X., Dumont, M.E. and Sherman, F. (1996) Sequence requirements for mitochondrial import of yeast cytochrome c. J. Biol. Chem., 271, 6594-6604.
61. Wertman, K.F., Drubin, D.G. and Bostein, D. (1992) Systematic mutational analysis of the yeast ACT1 gene. Genetics, 132, 337-350.
62. Wolf, E., Vassilev, A., Makino, Y., Sali, A., Nakatani, Y. and Burley, S.K. (1998) Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell, 94, 439-449.
63. α-acetyltranferase: isolation and characterization. Biochemistry, 30, 1010-1016.
64. α-acetyltranferase: substrate specificity. Biochemistry, 30, 1017-1021.
65. Yamamoto, T., Moerschell, R.P., Wakem, L.P., Ferguson, D. and Sherman, F. (1992) Parameters affecting the frequencies of transformation and co-transformation with synthetic oligonucleotides in yeast. Yeast, 8, 935-948.