TIP49, homologous to the bacterial DNA helicase RuvB, acts as an autoantigen in human
TIP49, homologous to the bacterial DNA helicase RuvB, acts as an autoantigen in human
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DOI:
10.1006/bbrc.1998.8504
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发表时间:
1998-04-28
影响因子:
3.1
通讯作者:
Tamura, T
中科院分区:
文献类型:
--
作者:
Makino, Y;Mimori, T;Tamura, T
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. (C) 1998 Academic Press.