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A promiscuous α-helical motif anchors viral hijackers and substrate receptors to the CUL4–DDB1 ubiquitin ligase machinery
- Ti Li, E. Robert, P. V. Breugel, M. Strubin, N. Zheng
- Biology, Medicine
- Nature Structural &Molecular Biology
The structure reveals that HBx binds DDB1 through an α-helical motif, which is also found in the unrelated paramyxovirus SV5-V protein despite their sequence divergence, and reveals a common yet promiscuous structural element that is important for the assembly of cellular and virally hijacked CUL4–DDB1 E3 complexes. Expand
OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins
Outstanding results show that expression of OBF-1 in HeLa cells selectively stimulates the activity of a natural immunoglobulin promoter in an octamer site-dependent manner and has all the properties expected for a B cell-specific transcriptional coactivator protein. Expand
Hepatitis B virus X protein identifies the Smc5/6 complex as a host restriction factor
A novel role for the Smc5/6 complex as a restriction factor selectively blocking extrachromosomal DNA transcription is uncovered, and HBx relieves the inhibition to allow productive hepatitis B virus gene expression. Expand
Hepatitis B Virus X Protein Stimulates Viral Genome Replication via a DDB1-Dependent Pathway Distinct from That Leading to Cell Death
It is shown that HBx in association with DDB1 acts in the nucleus and stimulates HBV replication mainly by enhancing viral mRNA levels, regardless of whether the protein is expressed from the HBV genome itself or supplied in trans. Expand
Histone chaperone spt16 promotes redeposition of the original h3-h4 histones evicted by elongating RNA polymerase.
It is shown that inactivation of histone chaperone Spt16 in yeast results in rapid loss of H2B and H3 from transcribed genes but also from inactive genes, and histone loss is blocked by a transcription inhibitor, indicating a transcription-dependent event. Expand
Yeast and human TFIID with altered DNA-binding specificity for TATA elements
These results define a surface of TFIID that directly interacts with the TATA element, and they indicate that human TFIIDs can respond to acidic activator proteins in conjunction with the other components of the yeast transcription machinery. Expand
A consensus motif in the RFX DNA binding domain and binding domain mutants with altered specificity.
- P. Emery, M. Strubin, K. Hofmann, P. Bucher, B. Mach, W. Reith
- Biology, Medicine
- Molecular and cellular biology
- 1 August 1996
The simplicity, efficiency, and versatility of the selection procedure developed make it of general value for the determination of consensus motifs, and for the isolation of mutants exhibiting altered functional properties, for large protein domains involved in protein-DNA as well as protein-protein interactions. Expand
The Large Subunit of Basal Transcription Factor SNAPc Is a Myb Domain Protein That Interacts with Oct-1
- M. W. Wong, R. W. Henry, +5 authors N. Hernandez
- Biology, Medicine
- Molecular and Cellular Biology
- 1 January 1998
The results suggest that the largest subunit of the SNAP complex is involved in direct recognition of the PSE and is a target for the Oct-1 activator, and provide an example of a basal transcription factor containing a Myb DNA binding domain. Expand
Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication.
It is inferred that replication-independent incorporation of H2B and H3 are distinct events, each occurring independently of the histone tail, and that nucleosome loss at active promoters reflects a dynamic equilibrium between histone deposition and dissociation. Expand
Stimulation of RNA polymerase II transcription initiation by recruitment of TBP in vivo
A novel strategy in yeast is used to show that a physical interaction with TBP is sufficient for a sequence-specific DNA-binding protein to increase initiation of transcription by RNA polymerase II, implying that binding of TFIID to promoter elements is a limiting step in transcription complex assembly in vivo. Expand