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Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation

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Standard

Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. / Haenni, Sandra S; Hassa, Paul O; Altmeyer, Matthias; Fey, Monika; Imhof, Ralph; Hottiger, Michael O.

I: International Journal of Biochemistry & Cell Biology, Bind 40, Nr. 10, 2008, s. 2274-83.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Haenni, SS, Hassa, PO, Altmeyer, M, Fey, M, Imhof, R & Hottiger, MO 2008, 'Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation', International Journal of Biochemistry & Cell Biology, bind 40, nr. 10, s. 2274-83. https://doi.org/10.1016/j.biocel.2008.03.008

APA

Haenni, S. S., Hassa, P. O., Altmeyer, M., Fey, M., Imhof, R., & Hottiger, M. O. (2008). Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. International Journal of Biochemistry & Cell Biology, 40(10), 2274-83. https://doi.org/10.1016/j.biocel.2008.03.008

Vancouver

Haenni SS, Hassa PO, Altmeyer M, Fey M, Imhof R, Hottiger MO. Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. International Journal of Biochemistry & Cell Biology. 2008;40(10):2274-83. https://doi.org/10.1016/j.biocel.2008.03.008

Author

Haenni, Sandra S ; Hassa, Paul O ; Altmeyer, Matthias ; Fey, Monika ; Imhof, Ralph ; Hottiger, Michael O. / Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. I: International Journal of Biochemistry & Cell Biology. 2008 ; Bind 40, Nr. 10. s. 2274-83.

Bibtex

@article{96ea753d39c8431fbfc980a314bae8cb,
title = "Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation",
abstract = "Poly-ADP-ribose polymerase-2 (PARP-2) was described to regulate cellular functions comprising DNA surveillance, inflammation and cell differentiation by co-regulating different transcription factors. Using an in vitro and in vivo approach, we identified PARP-2 as a new substrate for the histone acetyltransferases PCAF and GCN5L. Site directed mutagenesis indicated that lysines 36 and 37, located in the nuclear localization signal of PARP-2, are the main targets for PCAF and GCN5L activity in vitro. Interestingly, acetylation of the same two PARP-2 residues reduces the DNA binding and enzymatic activity of PARP-2. Finally, PARP-2 with mutated lysines 36 and 37 showed reduced auto-mono-ADP-ribosylation when compared to wild type PARP-2. Together, our results provide evidence that acetylation of PARP-2 is a key post-translational modification that may regulate DNA binding and consequently also the enzymatic activity of PARP-2.",
author = "Haenni, {Sandra S} and Hassa, {Paul O} and Matthias Altmeyer and Monika Fey and Ralph Imhof and Hottiger, {Michael O}",
year = "2008",
doi = "10.1016/j.biocel.2008.03.008",
language = "English",
volume = "40",
pages = "2274--83",
journal = "International Journal of Biochemistry & Cell Biology",
issn = "1357-2725",
publisher = "Elsevier",
number = "10",

}

RIS

TY - JOUR

T1 - Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation

AU - Haenni, Sandra S

AU - Hassa, Paul O

AU - Altmeyer, Matthias

AU - Fey, Monika

AU - Imhof, Ralph

AU - Hottiger, Michael O

PY - 2008

Y1 - 2008

N2 - Poly-ADP-ribose polymerase-2 (PARP-2) was described to regulate cellular functions comprising DNA surveillance, inflammation and cell differentiation by co-regulating different transcription factors. Using an in vitro and in vivo approach, we identified PARP-2 as a new substrate for the histone acetyltransferases PCAF and GCN5L. Site directed mutagenesis indicated that lysines 36 and 37, located in the nuclear localization signal of PARP-2, are the main targets for PCAF and GCN5L activity in vitro. Interestingly, acetylation of the same two PARP-2 residues reduces the DNA binding and enzymatic activity of PARP-2. Finally, PARP-2 with mutated lysines 36 and 37 showed reduced auto-mono-ADP-ribosylation when compared to wild type PARP-2. Together, our results provide evidence that acetylation of PARP-2 is a key post-translational modification that may regulate DNA binding and consequently also the enzymatic activity of PARP-2.

AB - Poly-ADP-ribose polymerase-2 (PARP-2) was described to regulate cellular functions comprising DNA surveillance, inflammation and cell differentiation by co-regulating different transcription factors. Using an in vitro and in vivo approach, we identified PARP-2 as a new substrate for the histone acetyltransferases PCAF and GCN5L. Site directed mutagenesis indicated that lysines 36 and 37, located in the nuclear localization signal of PARP-2, are the main targets for PCAF and GCN5L activity in vitro. Interestingly, acetylation of the same two PARP-2 residues reduces the DNA binding and enzymatic activity of PARP-2. Finally, PARP-2 with mutated lysines 36 and 37 showed reduced auto-mono-ADP-ribosylation when compared to wild type PARP-2. Together, our results provide evidence that acetylation of PARP-2 is a key post-translational modification that may regulate DNA binding and consequently also the enzymatic activity of PARP-2.

U2 - 10.1016/j.biocel.2008.03.008

DO - 10.1016/j.biocel.2008.03.008

M3 - Journal article

C2 - 18436469

VL - 40

SP - 2274

EP - 2283

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

SN - 1357-2725

IS - 10

ER -

ID: 43224524