A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin

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A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin. / Aygün, Ozan; Svejstrup, Jesper; Liu, Yilun.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 105, Nr. 25, 24.06.2008, s. 8580-8584.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Aygün, O, Svejstrup, J & Liu, Y 2008, 'A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin', Proceedings of the National Academy of Sciences of the United States of America, bind 105, nr. 25, s. 8580-8584. https://doi.org/10.1073/pnas.0804424105

APA

Aygün, O., Svejstrup, J., & Liu, Y. (2008). A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin. Proceedings of the National Academy of Sciences of the United States of America, 105(25), 8580-8584. https://doi.org/10.1073/pnas.0804424105

Vancouver

Aygün O, Svejstrup J, Liu Y. A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin. Proceedings of the National Academy of Sciences of the United States of America. 2008 jun. 24;105(25):8580-8584. https://doi.org/10.1073/pnas.0804424105

Author

Aygün, Ozan ; Svejstrup, Jesper ; Liu, Yilun. / A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin. I: Proceedings of the National Academy of Sciences of the United States of America. 2008 ; Bind 105, Nr. 25. s. 8580-8584.

Bibtex

@article{d4b2fd8a958a4ce7b7d1ea17f1b47050,
title = "A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin",
abstract = "Although the active forms of factors involved in DNA-related processes such as DNA replication, repair, and transcription are associated with chromatin, proteins are rarely purified from this source. Here, we describe a protocol for the isolation of chromatin-associated factors and use it to identify proteins interacting with human RNA polymerase II (RNAPII). Our data establish RECQ5 helicase as a bona fide RNAPII-associated protein. The RECQ5-RNAPII interaction is direct and is mediated by the RPB1 subunit of RNAPII, and RECQ5 appears to be the only member of the human RECQ family of helicases that associates with RNAPII. These data suggest an unexpected role for RECQ5 helicase at the interface of transcription and genomic stability.",
keywords = "BLM, Genome integrity, Transcription, WRN",
author = "Ozan Ayg{\"u}n and Jesper Svejstrup and Yilun Liu",
year = "2008",
month = jun,
day = "24",
doi = "10.1073/pnas.0804424105",
language = "English",
volume = "105",
pages = "8580--8584",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "25",

}

RIS

TY - JOUR

T1 - A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin

AU - Aygün, Ozan

AU - Svejstrup, Jesper

AU - Liu, Yilun

PY - 2008/6/24

Y1 - 2008/6/24

N2 - Although the active forms of factors involved in DNA-related processes such as DNA replication, repair, and transcription are associated with chromatin, proteins are rarely purified from this source. Here, we describe a protocol for the isolation of chromatin-associated factors and use it to identify proteins interacting with human RNA polymerase II (RNAPII). Our data establish RECQ5 helicase as a bona fide RNAPII-associated protein. The RECQ5-RNAPII interaction is direct and is mediated by the RPB1 subunit of RNAPII, and RECQ5 appears to be the only member of the human RECQ family of helicases that associates with RNAPII. These data suggest an unexpected role for RECQ5 helicase at the interface of transcription and genomic stability.

AB - Although the active forms of factors involved in DNA-related processes such as DNA replication, repair, and transcription are associated with chromatin, proteins are rarely purified from this source. Here, we describe a protocol for the isolation of chromatin-associated factors and use it to identify proteins interacting with human RNA polymerase II (RNAPII). Our data establish RECQ5 helicase as a bona fide RNAPII-associated protein. The RECQ5-RNAPII interaction is direct and is mediated by the RPB1 subunit of RNAPII, and RECQ5 appears to be the only member of the human RECQ family of helicases that associates with RNAPII. These data suggest an unexpected role for RECQ5 helicase at the interface of transcription and genomic stability.

KW - BLM

KW - Genome integrity

KW - Transcription

KW - WRN

U2 - 10.1073/pnas.0804424105

DO - 10.1073/pnas.0804424105

M3 - Journal article

C2 - 18562274

AN - SCOPUS:47249100637

VL - 105

SP - 8580

EP - 8584

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 25

ER -

ID: 331006916