|
|
|
|
| LEADER |
00000nam a22000003u 4500 |
| 001 |
b6978672 |
| 003 |
CoU |
| 005 |
20091216000000.0 |
| 006 |
m d f |
| 007 |
cr ||||||||||| |
| 008 |
110824e20010410cau o| f0|||||eng|d |
| 035 |
|
|
|a (TOE)ost860724
|
| 035 |
|
|
|a (TOE)860724
|
| 040 |
|
|
|a TOE
|c TOE
|
| 049 |
|
|
|a GDWR
|
| 072 |
|
7 |
|a 59
|2 edbsc
|
| 086 |
0 |
|
|a E 1.99:lbnl--47730
|
| 086 |
0 |
|
|a E 1.99:lbnl--47730
|
| 088 |
|
|
|a lbnl--47730
|
| 245 |
0 |
0 |
|a Defining interactions between DNA-PK and ligase IV/XRCC4
|h [electronic resource]
|
| 260 |
|
|
|a Berkeley, Calif. :
|b Lawrence Berkeley National Laboratory ;
|a Oak Ridge, Tenn. :
|b distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy,
|c 2001.
|
| 336 |
|
|
|a text
|b txt
|2 rdacontent.
|
| 337 |
|
|
|a computer
|b c
|2 rdamedia.
|
| 338 |
|
|
|a online resource
|b cr
|2 rdacarrier.
|
| 500 |
|
|
|a Published through the Information Bridge: DOE Scientific and Technical Information.
|
| 500 |
|
|
|a 04/10/2001.
|
| 500 |
|
|
|a "lbnl--47730"
|
| 500 |
|
|
|a DNA Repair 1 3 FT.
|
| 500 |
|
|
|a Journal Publication Date: 03/28/2002.
|
| 500 |
|
|
|a Chen, David J.; Hsu, Hsin-Ling; Yannone, Steven M.
|
| 500 |
|
|
|a USDOE Director, Office of Science. Office of Biological andEnvironmental Research. Life Sciences Division.
|
| 500 |
|
|
|a National Institutes ofHealth.
|
| 520 |
3 |
|
|a Non-homologous end joining (NHEJ) is a major pathway for the repair of DNA double-strand breaks in mammalian cells. DNA-dependent protein kinase (DNA-PK), ligase IV, and XRCC4 are all critical components of the NHEJ repair pathway. DNA-PK is composed of a heterodimeric DNA-binding component, Ku, and a large catalytic subunit, DNA-PKcs. Ligase IV and XRCC4 associate to form a multimeric complex that is also essential for NHEJ. DNA-PK and ligase IV/XRCC4 interact at DNA termini which results in stimulated ligase activity. Here we define interactions between the components of these two essential complexes, DNA-PK and ligase IV/XRCC4. We find that ligase IV/XRCC4 associates with DNA-PK in a DNA-independent manner. The specific protein-protein interactions that mediate the interaction between these two complexes are further identified. Direct physical interactions between ligase IV and Ku as well as between XRCC4 and DNA-PKcs are shown. No direct interactions are observed between ligase IV and DNA-PKcs or between XRCC4 and Ku. Our data defines the specific protein pairs involved in the association of DNA-PK and ligase IV/XRCC4, and suggests a molecular mechanism for coordinating the assembly of the DNA repair complex at DNA breaks.
|
| 536 |
|
|
|b DE-AC02-05CH11231.
|
| 536 |
|
|
|b NIH:AG917709.
|
| 536 |
|
|
|b CA50519.
|
| 536 |
|
|
|b 440803.
|
| 650 |
|
7 |
|a Biological Pathways.
|2 local.
|
| 650 |
|
7 |
|a Repair.
|2 local.
|
| 650 |
|
7 |
|a Ligases.
|2 local.
|
| 650 |
|
7 |
|a Dna.
|2 local.
|
| 650 |
|
7 |
|a Proteins.
|2 local.
|
| 650 |
|
7 |
|a Dna Repair.
|2 local.
|
| 650 |
|
7 |
|a Phosphotransferases.
|2 local.
|
| 650 |
|
7 |
|a Basic Biological Sciences.
|2 edbsc.
|
| 710 |
2 |
|
|a Lawrence Berkeley National Laboratory.
|4 res.
|
| 710 |
1 |
|
|a United States.
|b Department of Energy.
|b Office of Scientific and Technical Information.
|4 dst.
|
| 856 |
4 |
0 |
|u http://www.osti.gov/servlets/purl/860724-sVO9h3/
|z Online Access
|
| 907 |
|
|
|a .b69786720
|b 03-06-23
|c 03-31-12
|
| 998 |
|
|
|a web
|b 03-31-12
|c f
|d m
|e p
|f eng
|g cau
|h 0
|i 1
|
| 956 |
|
|
|a Information bridge
|
| 999 |
f |
f |
|i 7ddf2f49-c113-55b0-932f-10bb5d4f3882
|s ef44aa54-91ee-5789-9427-6f198a51042d
|
| 952 |
f |
f |
|p Can circulate
|a University of Colorado Boulder
|b Online
|c Online
|d Online
|e E 1.99:lbnl--47730
|h Superintendent of Documents classification
|i web
|n 1
|
