DDB1

Official Full Name

damage specific DNA binding protein 1

Organism

Homo sapiens

GeneID

1642

Background

The protein encoded by this gene is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex while another protein (p48) forms the small subunit. This protein complex functions in nucleotide-excision repair and binds to DNA following UV damage. Defective activity of this complex causes the repair defect in patients with xeroderma pigmentosum complementation group E (XPE) - an autosomal recessive disorder characterized by photosensitivity and early onset of carcinomas. However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform mascular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients. The protein encoded by this gene also functions as an adaptor molecule for the cullin 4 (CUL4) ubiquitin E3 ligase complex by facilitating the binding of substrates to this complex and the ubiquitination of proteins. [provided by RefSeq, May 2012]

Synonyms

XPE; DDBA; XAP1; XPCE; XPE-BF; UV-DDB1; WHIKERS;

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Detailed Information

The maintenance of genetic stability is a crucial process in cells, as it ensures the accurate transmission of genetic information from one generation to the next. This process is complicated by the constant exposure of DNA to various endogenous and exogenous factors that can cause DNA damage. Therefore, cells have evolved a complex DNA repair machinery to identify and repair damaged DNA, preventing genetic instability and the development of diseases such as cancer. Damage-specific DNA binding protein 1 (DDB1) is a crucial player in the cellular response to DNA damage, functioning as a sensor for DNA lesions and recruiting additional proteins to facilitate DNA repair.

Structure and Organization of DDB1

DDB1 is a member of the Chromatin-Modifying Enzyme (CSE) family, which is characterized by the presence of a highly conserved C-terminal domain and a variable N-terminal domain. The structure of DDB1 has been extensively studied, revealing a unique dimeric architecture consisting of two distinct domains: the N-terminal DNA-binding domain (N-DDB) and the C-terminal binding domain (C-DDB). The N-DDB domain is responsible for recognizing specific DNA lesions, while the C-DDB domain mediates the interaction with other DNA repair proteins.

Functional Role of DDB1 in DNA Repair

The primary function of DDB1 is to detect and bind to DNA lesions, thereby initiating the recruitment of additional DNA repair proteins to the damaged site. Upon binding to damaged DNA, DDB1 forms a complex with other DNA repair factors, such as the DNA damage inducible transcript 3 (DICT3) and the Cockayne's syndrome protein A (CSA), to facilitate the repair of DNA lesions. The complex formation is essential for the recruitment of the DNA repair machinery to the damaged site, ensuring the accurate repair of DNA and maintaining genetic stability.

DDB1 and Human Diseases

Impairments in the DNA repair machinery can have severe consequences for human health, as they lead to an increased accumulation of DNA damage and genetic instability. Consequently, mutations in the DDB1 gene have been associated with various human diseases, including cancer, neurodegenerative disorders, and immunological defects. For instance, mutations in the DDB1 gene have been identified as a cause of Cockayne's syndrome, a rare autosomal recessive disorder characterized by defects in DNA repair, premature aging, and neurological degeneration. Moreover, defects in DDB1 function have been implicated in the development of cancer, as they can lead to an increased mutation rate and genome instability.

References:

Iovine, Barbara et al. "Damage-specific DNA binding protein 1 (DDB1): a protein with a wide range of functions." The international journal of biochemistry & cell biology vol. 43,12 (2011): 1664-7. doi:10.1016/j.biocel.2011.09.001
Iovine, Barbara et al. "Damage-specific DNA binding protein 1 (DDB1) is involved in ubiquitin-mediated proteolysis of p27Kip1 in response to UV irradiation." Biochimie vol. 93,5 (2011): 867-75. doi:10.1016/j.biochi.2010.12.017

Quick Inquiry

Interested in learning more?

Contact us today for a free consultation with the scientific team and discover how Creative Biogene can be a valuable resource and partner for your organization.

Request a quote today!

Inquiry