PMID- 16260596
OWN - NLM
STAT- MEDLINE
DCOM- 20051216
LR  - 20181113
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 25
IP  - 22
DP  - 2005 Nov
TI  - Xeroderma pigmentosum complementation group E protein (XPE/DDB2): purification of 
      various complexes of XPE and analyses of their damaged DNA binding and putative 
      DNA repair properties.
PG  - 9784-92
AB  - Xeroderma pigmentosum is characterized by increased sensitivity of the affected 
      individuals to sunlight and light-induced skin cancers and, in some cases, to 
      neurological abnormalities. The disease is caused by a mutation in genes XPA 
      through XPG and the XP variant (XPV) gene. The proteins encoded by the XPA, -B, 
      -C, -D, -F, and -G genes are required for nucleotide excision repair, and the XPV 
      gene encodes DNA polymerase eta, which carries out translesion DNA synthesis. In 
      contrast, the mechanism by which the XPE gene product prevents sunlight-induced 
      cancers is not known. The gene (XPE/DDB2) encodes the small subunit of a 
      heterodimeric DNA binding protein with high affinity to UV-damaged DNA 
      (UV-damaged DNA binding protein [UV-DDB]). The DDB2 protein exists in at least 
      four forms in the cell: monomeric DDB2, DDB1-DDB2 heterodimer (UV-DDB), and as a 
      protein associated with both the Cullin 4A (CUL4A) complex and the COP9 
      signalosome. To better define the role of DDB2 in the cellular response to DNA 
      damage, we purified all four forms of DDB2 and analyzed their DNA binding 
      properties and their effects on mammalian nucleotide excision repair. We find 
      that DDB2 has an intrinsic damaged DNA binding activity and that under our assay 
      conditions neither DDB2 nor complexes that contain DDB2 (UV-DDB, CUL4A, and COP9) 
      participate in nucleotide excision repair carried out by the six-factor human 
      excision nuclease.
FAU - Kulaksiz, Gulnihal
AU  - Kulaksiz G
AD  - Biyokimya Anabilim Dali, Hacettepe Universitesi Tip Fakultesi, Ankara, Turkey.
FAU - Reardon, Joyce T
AU  - Reardon JT
FAU - Sancar, Aziz
AU  - Sancar A
LA  - eng
GR  - R01 GM032833/GM/NIGMS NIH HHS/United States
GR  - GM32833/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (DDB2 protein, human)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Multiprotein Complexes)
RN  - 9007-49-2 (DNA)
RN  - EC 2.7.7.7 (DNA-Directed DNA Polymerase)
RN  - EC 2.7.7.7 (Rad30 protein)
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.19.12 (COP9 Signalosome Complex)
SB  - IM
MH  - Animals
MH  - Apoptosis
MH  - CHO Cells
MH  - COP9 Signalosome Complex
MH  - Cell Cycle
MH  - Cell Line
MH  - Chromatography, Affinity
MH  - Cricetinae
MH  - DNA/*chemistry
MH  - *DNA Damage
MH  - *DNA Repair
MH  - DNA-Binding Proteins/*genetics/*physiology
MH  - DNA-Directed DNA Polymerase/chemistry
MH  - Dimerization
MH  - Dose-Response Relationship, Drug
MH  - Humans
MH  - Insecta
MH  - Multiprotein Complexes/metabolism
MH  - Peptide Hydrolases/metabolism
MH  - Ultraviolet Rays
PMC - PMC1280284
EDAT- 2005/11/02 09:00
MHDA- 2005/12/17 09:00
PMCR- 2005/11/01
CRDT- 2005/11/02 09:00
PHST- 2005/11/02 09:00 [pubmed]
PHST- 2005/12/17 09:00 [medline]
PHST- 2005/11/02 09:00 [entrez]
PHST- 2005/11/01 00:00 [pmc-release]
AID - 25/22/9784 [pii]
AID - 1536-05 [pii]
AID - 10.1128/MCB.25.22.9784-9792.2005 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2005 Nov;25(22):9784-92. doi: 10.1128/MCB.25.22.9784-9792.2005.