Purification and characterization of the human elongator complex

Research output: Contribution to journal › Journal article › Research › peer-review

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Purification and characterization of the human elongator complex. / Hawkes, Nicola A.; Otero, Gabriel; Sebastiaan Winkler, G.; Marshall, Nick; Dahmus, Michael E.; Krappmann, Daniel; Scheidereit, Claus; Thomas, Claire L.; Schiavo, Giampietro; Erdjument-Bromage, Hediye; Svejstrup, Jesper Q.

In: Journal of Biological Chemistry, Vol. 277, No. 4, 25.01.2002, p. 3047-3052.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hawkes, NA, Otero, G, Sebastiaan Winkler, G, Marshall, N, Dahmus, ME, Krappmann, D, Scheidereit, C, Thomas, CL, Schiavo, G, Erdjument-Bromage, H & Svejstrup, JQ 2002, 'Purification and characterization of the human elongator complex', Journal of Biological Chemistry, vol. 277, no. 4, pp. 3047-3052. https://doi.org/10.1074/jbc.M110445200

APA

Hawkes, N. A., Otero, G., Sebastiaan Winkler, G., Marshall, N., Dahmus, M. E., Krappmann, D., Scheidereit, C., Thomas, C. L., Schiavo, G., Erdjument-Bromage, H., & Svejstrup, J. Q. (2002). Purification and characterization of the human elongator complex. Journal of Biological Chemistry, 277(4), 3047-3052. https://doi.org/10.1074/jbc.M110445200

Vancouver

Hawkes NA, Otero G, Sebastiaan Winkler G, Marshall N, Dahmus ME, Krappmann D et al. Purification and characterization of the human elongator complex. Journal of Biological Chemistry. 2002 Jan 25;277(4):3047-3052. https://doi.org/10.1074/jbc.M110445200

Author

Hawkes, Nicola A. ; Otero, Gabriel ; Sebastiaan Winkler, G. ; Marshall, Nick ; Dahmus, Michael E. ; Krappmann, Daniel ; Scheidereit, Claus ; Thomas, Claire L. ; Schiavo, Giampietro ; Erdjument-Bromage, Hediye ; Svejstrup, Jesper Q. / Purification and characterization of the human elongator complex. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 4. pp. 3047-3052.

Bibtex

@article{5621496b4a2648e0a5cd33780bec441f,
title = "Purification and characterization of the human elongator complex",
abstract = "Human Elongator complex was purified to virtual homogeneity from HeLa cell extracts. The purified factor can exist in two forms: a six-subunit complex, holo-Elongator, which has histone acetyltransferase activity directed against histone H3 and H4, and a three-subunit core form, which does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit. Elongator is a component of early elongation complexes formed in HeLa nuclear extracts and can interact directly with RNA polymerase II in solution. Several human homologues of the yeast Elongator subunits were identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein). Mutations in IKAP can result in the severe human disorder familial dysautonomia, raising the possibility that this disease might be due to compromised Elongator function and therefore could be a transcription disorder.",
author = "Hawkes, {Nicola A.} and Gabriel Otero and {Sebastiaan Winkler}, G. and Nick Marshall and Dahmus, {Michael E.} and Daniel Krappmann and Claus Scheidereit and Thomas, {Claire L.} and Giampietro Schiavo and Hediye Erdjument-Bromage and Svejstrup, {Jesper Q.}",
year = "2002",
month = jan,
day = "25",
doi = "10.1074/jbc.M110445200",
language = "English",
volume = "277",
pages = "3047--3052",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "4",

}

RIS

TY - JOUR

T1 - Purification and characterization of the human elongator complex

AU - Hawkes, Nicola A.

AU - Otero, Gabriel

AU - Sebastiaan Winkler, G.

AU - Marshall, Nick

AU - Dahmus, Michael E.

AU - Krappmann, Daniel

AU - Scheidereit, Claus

AU - Thomas, Claire L.

AU - Schiavo, Giampietro

AU - Erdjument-Bromage, Hediye

AU - Svejstrup, Jesper Q.

PY - 2002/1/25

Y1 - 2002/1/25

N2 - Human Elongator complex was purified to virtual homogeneity from HeLa cell extracts. The purified factor can exist in two forms: a six-subunit complex, holo-Elongator, which has histone acetyltransferase activity directed against histone H3 and H4, and a three-subunit core form, which does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit. Elongator is a component of early elongation complexes formed in HeLa nuclear extracts and can interact directly with RNA polymerase II in solution. Several human homologues of the yeast Elongator subunits were identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein). Mutations in IKAP can result in the severe human disorder familial dysautonomia, raising the possibility that this disease might be due to compromised Elongator function and therefore could be a transcription disorder.

AB - Human Elongator complex was purified to virtual homogeneity from HeLa cell extracts. The purified factor can exist in two forms: a six-subunit complex, holo-Elongator, which has histone acetyltransferase activity directed against histone H3 and H4, and a three-subunit core form, which does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit. Elongator is a component of early elongation complexes formed in HeLa nuclear extracts and can interact directly with RNA polymerase II in solution. Several human homologues of the yeast Elongator subunits were identified as subunits of the human Elongator complex, including StIP1 (STAT-interacting protein 1) and IKAP (IKK complex-associated protein). Mutations in IKAP can result in the severe human disorder familial dysautonomia, raising the possibility that this disease might be due to compromised Elongator function and therefore could be a transcription disorder.

U2 - 10.1074/jbc.M110445200

DO - 10.1074/jbc.M110445200

M3 - Journal article

C2 - 11714725

AN - SCOPUS:0037169503

VL - 277

SP - 3047

EP - 3052

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 4

ER -

ID: 331041790