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Molecular and Cellular Biology, September 2002, p. 6564-6572, Vol. 22, No. 18
0270-7306/02/$04.00+0 DOI: 10.1128/MCB.22.18.6564-6572.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Department of Molecular and Cell Biology,1 Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, California 94720-32042
Received 18 March 2002/ Returned for modification 10 May 2002/ Accepted 12 June 2002
Regulated gene expression is a complex process achieved through the function of multiple protein factors acting in concert at a given promoter. The transcription factor TFIID is a central component of the machinery regulating mRNA synthesis by RNA polymerase II. This large multiprotein complex is composed of the TATA box binding protein (TBP) and several TBP-associated factors (TAFIIs). The recent discovery of multiple TBP-related factors and tissue-specific TAFIIs suggests the existence of specialized TFIID complexes that likely play a critical role in regulating transcription in a gene- and tissue-specific manner. The tissue-selective factor TAFII105 was originally identified as a component of TFIID derived from a human B-cell line. In this report we demonstrate the specific induction of TAFII105 in cultured B cells in response to bacterial lipopolysaccharide (LPS). To examine the in vivo role of TAFII105, we have generated TAFII105-null mice by homologous recombination. Here we show that B-lymphocyte development is largely unaffected by the absence of TAFII105. TAFII105-null B cells can proliferate in response to LPS, produce relatively normal levels of resting antibodies, and can mount an immune response by producing antigen-specific antibodies in response to immunization. Taken together, we conclude that the function of TAFII105 in B cells is likely redundant with the function of other TAFII105-related cellular proteins.
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