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J Biol Chem, Vol. 274, Issue 50, 35309-35312, December 10, 1999
From the Department of Biochemistry and Molecular Biology (M/C
536), University of Illinois, Chicago, Illinois 60612
The damaged DNA-binding protein (DDB) is believed
to be involved in DNA repair, and it has been linked to the repair
deficiency disease xeroderma pigmentosum. DDB also exhibits
transcriptional activities. DDB binds to the activation domain of E2F1
and stimulates E2F1-activated transcription. Here we provide evidence
that DDB or DDB-associated proteins are targets of cullin 4A (CUL-4A). CUL-4A is a member of the cullin family of proteins, which are believed
to be ubiquitin-protein isopeptide ligases (type E3). The CUL-4A gene
has been shown to be amplified and up-regulated in breast carcinomas.
In this study, we identify CUL-4A as one of the DDB-associated
proteins. CUL-4A co-immunoprecipitates with DDB, but not with a
naturally occurring mutant of DDB. Moreover, CUL-4A in HeLa nuclear
extracts co-purifies with DDB, suggesting they are parts of the same
complex. The observation provides insights how CUL-4A, through an
interaction with DDB, might be playing a role in the development of
breast carcinomas.
To whom correspondence should be addressed. Tel.: 312-413-0255;
Fax: 312-413-0364; E-mail: pradip@uic.edu.
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