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Vol. 9, No. 4, 2002
Issue release date: July–August 2002
Section title: Original Paper
J Biomed Sci 2002;9:371–380
(DOI:10.1159/000065009)

Identification of Rat DDB1, a Putative DNA Repair Protein, and Functional Correlation with Its Damaged-DNA Recognition Activity

Khallaf F.G.M. · Sun N.K.a,b · Lu H.P.a · Al-Akkd M.T. · Al-Kussary I.M. · Chao C.C.K.a · Al-Mi Kami A.
aTumor Biology Laboratory, Department of Biochemistry, Chang Gung, University, Taoyuan, and bInstitute of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan, ROC

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Published online: 7/19/2002
Issue release date: July–August 2002

Number of Print Pages: 10
Number of Figures: 8
Number of Tables: 0

ISSN: 1021-7770 (Print)
eISSN: 1423-0127 (Online)

For additional information: http://www.karger.com/JBS

Abstract

Recognition and incision of UV-DNA adducts play key roles in the efficacy of nucleotide excision repair. Damaged-DNA recognition activity has been identified from primate cells as a complex of DDB1 (127-kD) and DDB2 (48-kD) subunits. However, the function of damaged-DNA binding proteins (DDBs) in damaged-DNA recognition is not well understood. To assess the functional correlation between DDBs and UV-damaged-DNA recognition activity, we identified UV-damaged-DNA recognition activities in rodent cell lines. There is a cell type-dependent expression of DDB1 and DDB2. Rodent cells had less abundant DDBs and lower UV-damaged-DNA recognition activity than did human tumor cells. Interestingly, the profusion of DDBs is associated with UV-damaged-DNA recognition activity in these cell lines. We also discovered tissue-dependent expression of DDBs and its functional correlation with UV-damaged-DNA recognition activity. cDNA (3850 nucleotides) from rat ddb1 was isolated. It contained the complete length of the open reading frame that encodes an 1140-amino-acid polypeptide with a predicted molecular weight of 126.8 kD. The predicted protein size from the rat ddb1 gene resembles that from human DDB1 (127 kD). Rat DDB1 shares highly conserved sequencing (greater than 98% similarity) with those of mouse, human, and monkey. Rat and fruit fly DDB1 exhibit 62.23% identity and 57.66% homology. The evolutionary conservation of the DDB1 sequence suggests that DDB1 may play a pivotal role in mammals as well as in other eukaryotes. However, overexpression of DDB1 did not augment UV-damaged-DNA recognition activity in human HeLa, hamster V79, or rat PC12 cells. In contrast, restricting DDB2 expression by antisense ddb2 partially inhibited UV-damaged-DNA recognition activity in cells, whereas overexpressing DDB2 through a recombinant ddb2 adenovirus partly restored the recognition activity of these cells. These findings support the notion that DDB abundance is functionally correlated with UV-damaged-DNA recognition activity. These results also suggest that the profusion of DDB2, but not DDB1, may moderate UV-damaged-DNA recognition activity.


  

Author Contacts

Chuck C.K. Chao
Tumor Biology Laboratory
Department of Biochemistry, Chang Gung University
Taoyuan, Taiwan 33332 (ROC)
Fax +886 3 3283031, E-Mail cckchao@mail.cgu.edu.tw

  

Article Information

Received: Received: December 11, 2001
Accepted: February 18, 2002
Number of Print Pages : 10
Number of Figures : 8, Number of Tables : 0, Number of References : 44

  

Publication Details

Journal of Biomedical Science (Sponsored by the National Science Council, Taipei)

Vol. 9, No. 4, Year 2002 (Cover Date: July-August 2002)

Journal Editor: S.H.H.Chan, Kaohsiung
ISSN: 1021–7770 (print), 1423–0127 (Online)

For additional information: http://www.karger.com/journals/jbs


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Published online: 7/19/2002
Issue release date: July–August 2002

Number of Print Pages: 10
Number of Figures: 8
Number of Tables: 0

ISSN: 1021-7770 (Print)
eISSN: 1423-0127 (Online)

For additional information: http://www.karger.com/JBS


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