TY - JOUR
T1 - A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein
AU - Takao, Masashi
AU - Abramic, Marija
AU - Moos, Malcolm
AU - Rapic' Otrin, Vesna
AU - Wootton, John C.
AU - Mclenigan, Mary
AU - Levine, Arthur S.
AU - Protic, Miroslava
PY - 1993/8/25
Y1 - 1993/8/25
N2 - A cDNA which encodes á 127 kDa UV-damaged DNA-binding (UV-DDB) protein with high affinity for (6-4)pyrlmidine dimers [Abramic', M., Levine, A.S. & Protic', M., J. Biol. Chem. 266:22493-22500,1991] has been Isolated from a monkey cell cDNA library. The presence of this protein in complexes bound to UV-damaged DNA was confirmed by immunobiotting. The human cognate of the UV-DDB gene was localized to chromosome 11. UV-DDB mRNA was expressed in all human tissues examined, including cells from two patients with xeroderma pigmentosum (group E) that are deficient in UV-DDB activity, which suggests that the binding defect in these cells may reside in a dysfunctional UV-DDB protein. Database searches have revealed significant homology of the UV-DDB protein sequence with partial sequences of yet uncharacterized proteins from Dictyostellum discoldeum (44% Identity over 529 amino acids) and Oryza satlva (54% identity over 74 residues). According to our results, the UV-DDB polypeptide belongs to a highly conserved, structurally novel family of proteins that may be involved in the early steps of the UV response, e.g., DNA damage recognition.
AB - A cDNA which encodes á 127 kDa UV-damaged DNA-binding (UV-DDB) protein with high affinity for (6-4)pyrlmidine dimers [Abramic', M., Levine, A.S. & Protic', M., J. Biol. Chem. 266:22493-22500,1991] has been Isolated from a monkey cell cDNA library. The presence of this protein in complexes bound to UV-damaged DNA was confirmed by immunobiotting. The human cognate of the UV-DDB gene was localized to chromosome 11. UV-DDB mRNA was expressed in all human tissues examined, including cells from two patients with xeroderma pigmentosum (group E) that are deficient in UV-DDB activity, which suggests that the binding defect in these cells may reside in a dysfunctional UV-DDB protein. Database searches have revealed significant homology of the UV-DDB protein sequence with partial sequences of yet uncharacterized proteins from Dictyostellum discoldeum (44% Identity over 529 amino acids) and Oryza satlva (54% identity over 74 residues). According to our results, the UV-DDB polypeptide belongs to a highly conserved, structurally novel family of proteins that may be involved in the early steps of the UV response, e.g., DNA damage recognition.
UR - http://www.scopus.com/inward/record.url?scp=0027203512&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027203512&partnerID=8YFLogxK
U2 - 10.1093/nar/21.17.4111
DO - 10.1093/nar/21.17.4111
M3 - Article
C2 - 8371985
AN - SCOPUS:0027203512
SN - 0305-1048
VL - 21
SP - 4111
EP - 4118
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 17
ER -