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Ku stimulation of DNA ligase IV-dependent ligation requires inward movement along the DNA molecule.

Abstract:

The DNA ligase IV.XRCC4 complex (LX) functions in DNA non-homologous-end joining, the main pathway for double-strand break repair in mammalian cells. We show that, in contrast to ligation by T4 ligase, the efficiency of LX ligation of double-stranded (ds) ends is critically dependent upon the length of the DNA substrate. The effect is specific for ds ligation, and LX/DNA binding is not influenced by the substrate length. Ku stimulates LX ligation at concentrations resulting in 1-2 Ku molecule...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m303273200

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Journal:
Journal of biological chemistry More from this journal
Volume:
278
Issue:
25
Pages:
22466-22474
Publication date:
2003-06-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Language:
English
Keywords:
Pubs id:
pubs:131372
UUID:
uuid:b7ef7f46-e36d-4010-9dbb-1996de9e633f
Local pid:
pubs:131372
Source identifiers:
131372
Deposit date:
2013-11-17

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