Expression, purification and proteomic analysis of recombinant histone H4 acetylated at lysine 16

Proteomics

Volumn 13, Issue 10-11, 2013, Pages 1687-1691

  Kallappagoudar, Satish ^a   Dammer, Eric B ^b   Duong, Duc Minh ^b   Seyfried, Nicholas T ^b   Lucchesi, John C ^a  

^a EMORY UNIVERSITY   (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Gene expression; Histone; Nucleosome; Technology

Indexed keywords

AMBER; HISTONE H4; LYSINE; TRANSFER RNA;

ALKYLATION; ARTICLE; CODON; DERIVATIZATION; DNA SEQUENCE; HISTONE ACETYLATION; HISTONE MODIFICATION; IONIZATION; MUTAGENESIS; NONHUMAN; NUCLEOSOME; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEOMICS; STOP CODON;

ACETYLATION; AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; CODON, TERMINATOR; ESCHERICHIA COLI; HISTONES; HUMANS; LYSINE; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOMICS; RECOMBINANT PROTEINS; TANDEM MASS SPECTROMETRY;

EUKARYOTA;

EID: 84878651820     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300025     Document Type: Article

References (16)

1. Smith, E. R., Cayrou, C., Huang, R., Lane, W. S. et al., A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol. Cell. Biol. 2005, 25, 9175-9188.
2. Taipale, M., Rea, S., Richter, K., Vilar, A. et al., hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Mol. Cell. Biol. 2005, 25, 6798-6810.
3. Li, X., Corsa, C. A., Pan, P. W., Wu, L. et al., MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. Mol. Cell. Biol. 2010, 30, 5335-5347.
4. Sharma, G. G., So, S., Gupta, A., Kumar, R. et al., MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repair. Mol. Cell. Biol. 2010, 30, 3582-3595.
5. Krishnan, V., Chow, M. Z., Wang, Z., Zhang, L. et al., Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice. Proc. Natl. Acad. Sci. USA 2011, 108, 12325-12330.
6. Li, X., Li, L., Pandey, R., Byun, J. S. et al., The histone acetyltransferase MOF is a key regulator of the embryonic stem cell core transcriptional network. Cell. Stem. Cell. 2012, 11, 163-178.
7. Neumann, H., Hancock, S. M., Buning, R., Routh, A. et al., A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation. Mol. Cell. 2009, 36, 153-163.
8. Dunlap, D., Yokoyama, R., Ling, H., Sun, H. Y. et al., Distinct contributions of MSL complex subunits to the transcriptional enhancement responsible for dosage compensation in Drosophila. Nucleic. Acids. Res. 2012, 40, 11281-11291.
9. Grigoryev, S. A., Woodcock, C. L., Chromatin organization-the 30 nm fiber. Exp. Cell. Res. 2012, 318, 1448-1455.
10. Shogren-Knaak, M. A., Peterson, C. L., Creating designer histones by native chemical ligation. Methods Enzymol. 2004, 375, 62-76.
11. Allahverdi, A., Yang, R., Korolev, N., Fan, Y. et al., The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association. Nucleic. Acids Res. 2011, 39, 1680-1691.
12. Simon, M. D., Installation of site-specific methylation into histones using methyl lysine analogs. Curr. Protoc. Mol. Biol. 2010, 18, 1-10.
13. Simon, M. D., Chu, F., Racki, L. R., de la Cruz, C. C. et al., The site-specific installation of methyl-lysine analogs into recombinant histones. Cell 2007, 128, 1003-1012.
14. Neumann, H., Peak-Chew, S. Y., Chin, J. W., Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nat. Chem. Biol. 2008, 4, 232-234.
15. Luger, K., Rechsteiner, T. J., Richmond, T. J., Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol. Biol. 1999, 119, 1-16.
16. Garcia, B. A., Mollah, S., Ueberheide, B. M., Busby, S. A. et al., Chemical derivatization of histones for facilitated analysis by mass spectrometry. Nat. Protoc. 2007, 2, 933-938.