Properties of Nat4, an Nα-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4

Molecular and Cellular Biology

Volumn 29, Issue 11, 2009, Pages 2913-2924

  Polevoda, Bogdan ^a   Hoskins, Jason ^a   Sherman, Fred ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; AMITROLE; BENOMYL; CYTOCHROME C; CYTOCHROME C1; HISTONE H2A; HISTONE H4; ISOCYTOCHROME C1; N ACETYLTRANSFERASE A; N ACETYLTRANSFERASE B; N ACETYLTRANSFERASE C; N ACETYLTRANSFERASE D; SERINE; TIABENDAZOLE; UNCLASSIFIED DRUG; CYC1 PROTEIN, S CEREVISIAE; HISTONE; HYBRID PROTEIN; NAT4 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

ACETYLATION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; FUNGAL STRAIN; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; ALLELE; CHEMISTRY; CYTOLOGY; DENSITY GRADIENT CENTRIFUGATION; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; POLYSOME; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; PROTEIN TRANSPORT;

SACCHAROMYCES CEREVISIAE; TETRAHYMENA;

ACETYLATION; ACETYLTRANSFERASES; ALLELES; AMINO ACID SEQUENCE; CENTRIFUGATION, DENSITY GRADIENT; CYTOCHROMES C; HISTONES; MOLECULAR SEQUENCE DATA; MUTATION; PHENOTYPE; POLYRIBOSOMES; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY;

EID: 66349135032     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00147-08     Document Type: Article

References (48)

1. Arnold, R. J., B. Polevoda, J. P. Reilly, and F. Sherman. 1999. The action of N-terminal acetyltransferases on yeast ribosomal proteins. J. Biol. Chem. 274:37035-37040.
2. Augen, J., and F. Wold. 1986. How much sequence information is needed for the regulation of amino-terminal acetylation of eukaryotic proteins? Trends Biochem. Sci. 11:494-497. (Pubitemid 17222500)
3. Baim, S. B., D. F. Pietras, D. C. Eustice, and F. Sherman. 1985. A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c. Mol. Cell. Biol. 5:1839-1846.
4. Barber, C. M., F. B. Turner, Y. Wang, K. Hagstrom, S. D. Taverna, S. Mollah, B. Ueberheide, B. J. Meyer, D. F. Hunt, P. Cheung, and C. D. Allis. 2004. The enhancement of histone H4 and H2A serine 1 phosphorylation during mitosis and S-phase is evolutionarily conserved. Chromosoma 112:360-371. (Pubitemid 38828194)
5. Berndsen, C. E., W. Selleck, S. J. McBryant, J. C. Hansen, S. Tan, and J. M. Denu. 2007. Nucleosome recognition by the piccolo NuA4 histone acetyltransferase complex. Biochemistry 46:2091-2099. (Pubitemid 46355320)
6. Combet, C., C., Blanchet, C. Geourjon, and G. Deléage. 2000. NPS@: network protein sequence analysis. Trends Biochem. Sci. 25:147-150.
7. Corpet, F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890.
8. Dou, Y., and M. A. Gorovsky. 2000. Phosphorylation of linker histone H1 regulates gene expression in vivo by creating a charge patch. Mol. Cell 6:225-231.
9. Dou, Y., and M. A. Gorovsky. 2002. Regulation of transcription by H1 phosphorylation in Tetrahymena is position independent and requires clustered sites. Proc. Natl. Acad. Sci. USA 99:6142-6146.
10. Driessen, H. P., W. W. de Jong, G. I. Tesser, and H. Bloemendal. 1985. The mechanism of N-terminal acetylation of proteins. CRC Crit. Rev. Biochem. 18:281-325.
11. Dumont, M. E., A. J. Mathews, B. T. Nall, S. B. Baim, D. C. Eustice, and F. Sherman. 1990. Differential stability of two apo-isocytochromes c in the yeast Saccharomyces cerevisie. Deletions and replacements of omega loops in yeast iso-1-cytochrome c. J. Biol. Chem. 265:2733-2739.
12. Fetrow, J. S., T. S. Cardillo, and F. Sherman. 1989. Deletions and replacements of omega loops in yeast iso-1-cytochrome c. Proteins 6:372-381.
13. Flinta, C., B. Persson, H. Jörnvall, and G. von Heijne. 1986. Structures of N-terminally acetylated proteins. Eur. J. Biochem. 154:193-196.
14. α- acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 23:7403-7414.
15. α acetylation in Saccharomyces cerevisiae. Mol. Cell. Biol. 24:10300-10312.
16. Hermann, G. J., E. J. King, and J. M. Shaw. 1997. The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton. J. Cell Biol. 137:141-153. (Pubitemid 27167302)
17. Johnson, L. M., P. S. Kayne, E. S. Kahn, and M. Grunstein. 1990. Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 87:6286-6290. (Pubitemid 20259002)
18. Jörnvall, H. 1975. Acetylation of protein N-terminal amino groups structural observations on α-amino acetylated proteins. J. Theor. Biol. 55:1-12.
19. Kayne, P. S., U. J. Kim, M. Han, J. R. Mullen, F. Yoshizaki, and M. Grunstein. 1988. Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Cell 55:27-39.
20. Krishnamoorthy, T., X. Chen, J. Govin, W. L. Cheung, J. Dorsey, K. Schindler, E. Winter, C. D. Allis, V. Guacci, S. Khochbin, M. T. Fuller, and S. L. Berger. 2006. Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is conserved in fly and mouse spermatogenesis. Genes Dev. 20:2580-2592. (Pubitemid 44396842)
21. Moerschell, R. P., S. Tsunasawa, and F. Sherman. 1988. Transformation of yeast with synthetic oligonucleotides. Proc. Natl. Acad. Sci. USA 85:524-528.
22. Mullen, J. R., P. S. Kayne, R. P. Moerschell, S. Tsunasawa, M. Gribskov, M. Colavito-Shepanski, M. Grunstein, F. Sherman, and R. Sternglanz. 1989. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J. 8:2067-2075. (Pubitemid 19273535)
23. Park, E.-C., and J. W. Szostak. 1992. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 11:2087-2093.
24. α-terminal acetylation of yeast proteins by NatA. Yeast 25:513-527.
25. α-terminal acetylation of eukaryotic proteins. J. Biol. Chem. 275:36479-36482.
26. α-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p and Mak31p. J. Biol. Chem. 276:20154-20159.
27. Polevoda, B., and F. Sherman. 2003. Composition and function of eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 308:1-11.
28. Polevoda, B., and F. Sherman. 2003. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J. Mol. Biol. 325:595-622.
29. Polevoda, B., J. Norbeck, H. Takakura, A. Blomberg, and F. Sherman. 1999. Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae. EMBO J. 18:6155-6168.
30. α-terminal acetyltransferase and of actin and tropomyosin. J. Biol. Chem. 278:30686-30697.
31. α-terminal acetyltransferases are associated with ribosomes. J. Cell. Biochem. 103:492-508.
32. Ren, Q., and M. A. Gorovsky. 2001. Histone H2A. Z acetylation modulates an essential charge patch. Mol. Cell 7:1329-1335.
33. Ren, Q., and M. A. Gorovsky. 2003. The nonessential H2A N-terminal tail can function as an essential charge patch on the H2A. Z variant N-terminal tail. Mol. Cell. Biol. 23:2778-2789.
34. Rigaut, G., A. Shevchenko, B. Rutz, M. Wilm, M. Mann, and B. Séraphin. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17:1030-1032.
35. Schneider, B. L., W. Seufert, B. Steiner, Q. H. Yang, and A. B. Futcher. 1995. Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae. Yeast 11:1265-1274.
36. Sherman, F. 2002. Getting started with yeast. Methods Enzymol. 350:3-41. (Pubitemid 34619482)
37. Sherman, F., and P. P. Slonimski. 1964. Respiration-deficient mutants of yeast II. Biochim. Biophys. Acta 90:1-15.
38. Singer, J. M., and J. M. Shaw. 2003. Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast. Proc. Natl. Acad. Sci. USA 100:7644-7649.
39. α-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J. Biol. Chem. 278:38109-38112.
40. 2- terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae. J. Biol. Chem. 267:5442-5544.
41. 2 terminus is necessary for virus particle assembly. J. Biol. Chem. 267:20277-20281.
42. Tercero, J. C., J. D. Dinman, and R. B. Wickner. 1993. Yeast MAK3 N-acetyltransferase recognizes the N-terminal four amino acids of the major coat protein (gag) of the L-A double-stranded RNA virus. J. Bacteriol. 175:3192-3194. (Pubitemid 23148758)
43. Tse, C., T. Sera, A. P. Wolffe, and J. C. Hansen. 1998. Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III. Mol. Cell. Biol. 18:4629-4638.
44. Vetro, J. A., and Y. H. Chang. 2002. Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo. J. Cell. Biochem. 85:678-688. (Pubitemid 34462779)
45. Wang, X., J. J. Connelly, C. L. Wang, and R. Sternglanz. 2004. Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing. Genetics 168:547-551. (Pubitemid 39346616)
46. Wassarman, D. A., and F. Sauer. 2001. TAF(II)250: a transcription toolbox. J. Cell Sci. 114:2895-2902.
47. Yamamoto, T., R. P. Moerschell, L. P. Wakem, D. Ferguson, and F. Sherman. 1992. Parameters affecting the frequencies of transformation and cotransformation with synthetic oligonucleotides in yeast. Yeast 8:935-948.
48. Zinser, E. G., and G. Daum. 1995. Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast 11:493-536.