Tudor hooks up with DNA repair

Lorenzo Corsini; Michael Sattler

doi:10.1038/nsmb0207-98

Tudor hooks up with DNA repair

Lorenzo Corsini, Michael Sattler

Chair of Biomolecular NMR-Spectroscopy

Research output: Contribution to journal › Short survey › peer-review

17 Scopus citations

Abstract

Histone lysine methylation has a central role in transcriptional regulation and has recently been linked to DNA damage repair. Now it has been shown that the DNA damage repair factor 53BP1 is recruited to DNA double-strand breaks by its tandem tudor domain, which specifically recognizes histone H4 dimethylated at lysine 20.

Original language	English
Pages (from-to)	98-99
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	14
Issue number	2
DOIs	https://doi.org/10.1038/nsmb0207-98
State	Published - Feb 2007

Access to Document

10.1038/nsmb0207-98

Cite this

@article{37921ed17f3d466ea59a912f6526d1d6,

title = "Tudor hooks up with DNA repair",

abstract = "Histone lysine methylation has a central role in transcriptional regulation and has recently been linked to DNA damage repair. Now it has been shown that the DNA damage repair factor 53BP1 is recruited to DNA double-strand breaks by its tandem tudor domain, which specifically recognizes histone H4 dimethylated at lysine 20.",

author = "Lorenzo Corsini and Michael Sattler",

year = "2007",

month = feb,

doi = "10.1038/nsmb0207-98",

language = "English",

volume = "14",

pages = "98--99",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Research",

number = "2",

}

TY - JOUR

T1 - Tudor hooks up with DNA repair

AU - Corsini, Lorenzo

AU - Sattler, Michael

PY - 2007/2

Y1 - 2007/2

N2 - Histone lysine methylation has a central role in transcriptional regulation and has recently been linked to DNA damage repair. Now it has been shown that the DNA damage repair factor 53BP1 is recruited to DNA double-strand breaks by its tandem tudor domain, which specifically recognizes histone H4 dimethylated at lysine 20.

AB - Histone lysine methylation has a central role in transcriptional regulation and has recently been linked to DNA damage repair. Now it has been shown that the DNA damage repair factor 53BP1 is recruited to DNA double-strand breaks by its tandem tudor domain, which specifically recognizes histone H4 dimethylated at lysine 20.

UR - http://www.scopus.com/inward/record.url?scp=33846969140&partnerID=8YFLogxK

U2 - 10.1038/nsmb0207-98

DO - 10.1038/nsmb0207-98

M3 - Short survey

C2 - 17277801

AN - SCOPUS:33846969140

SN - 1545-9993

VL - 14

SP - 98

EP - 99

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 2

ER -

Tudor hooks up with DNA repair

Abstract

Access to Document

Other files and links

Fingerprint

Cite this