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TIP49, Homologous to the Bacterial DNA Helicase RuvB, Acts as an Autoantigen in Human

TATA-binding protein (TBP), a central component for transcriptional regulation, forms complexes with various transcription regulators. We have isolated a novel human cDNA for a 49-kD TBP-interacting protein (TIP49). The human TIP49 was highly homologous to bacterial RuvB proteins that function as a...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1998-04, Vol.245 (3), p.819-823
Main Authors: Makino, Yasutaka, Mimori, Tsuneyo, Koike, Chika, Kanemaki, Masato, Kurokawa, Yumiko, Inoue, Satoshi, Kishimoto, Toshihiko, Tamura, Taka-aki
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Language:English
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Summary:TATA-binding protein (TBP), a central component for transcriptional regulation, forms complexes with various transcription regulators. We have isolated a novel human cDNA for a 49-kD TBP-interacting protein (TIP49). The human TIP49 was highly homologous to bacterial RuvB proteins that function as a DNA helicase to promote branch migration of the Holliday junction. Immunofluorescence analysis using anti-TIP49 antibody showed a typical dot-shaped nuclear staining pattern, suggesting that TIP49 is included in a macromolecular structure in the nucleus and may participate in nuclear events such as transcription and recombination. Moreover, glycerol gradient analysis demonstrated that TIP49 is present in a macromolecular complex in nuclear extracts. Interestingly, we detected a high level of autoantibodies against TIP49 in sera of patients with autoimmune diseases such as polymyositis/dermatomyositis and autoimmune hepatitis. This indicates that the autoantibody against this protein is a new marker for particular connective tissue diseases. These findings provide further evidence that the macromolecular structures described above are targeted by an autoimmune mechanism. The anti-TIP49 antibodies can be useful probes for clinical diagnosis and for investigation of intranuclear structure.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.8504