Abstract
Temperature sensitive mutations in host cell factor 1 (HCF-1) arrest cells in the middle of the G1 phase of the cycle. We have shown that the highly conserved C-terminal WYF domain of HCF-1 protein interacts with the MYND domain of the PDCD2 protein. This inter-action is conserved between human HCF-1 and HCF-2 and the C. elegans HCF. Overexpression of PDCD2, which interacts with the N-CoR/mSin3A corepressor complexes, suppresses cotransfected HCF-1 complement-ation of a temperature lesion in the endogenous HCF-1 protein. Overexpression of domains of either PDCD2 or HCF-1, which should interfere with interactions between these two proteins, enhances the complementation.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis Regulatory Proteins
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Binding Sites
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Caenorhabditis elegans
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Caenorhabditis elegans Proteins
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Cells, Cultured
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Gene Deletion
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Genetic Complementation Test
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Host Cell Factor C1
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Humans
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Molecular Sequence Data
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Nuclear Proteins / metabolism*
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Nuclear Receptor Co-Repressor 1
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Precipitin Tests
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Protein Structure, Tertiary
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Proteins / genetics*
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Proteins / metabolism*
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Repressor Proteins / metabolism*
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Saccharomyces cerevisiae
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Sequence Homology, Amino Acid
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Transcription Factors*
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Two-Hybrid System Techniques
Substances
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Apoptosis Regulatory Proteins
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Caenorhabditis elegans Proteins
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HCFC1 protein, human
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Host Cell Factor C1
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NCOR1 protein, human
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Nuclear Proteins
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Nuclear Receptor Co-Repressor 1
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PDCD2 protein, human
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Proteins
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Repressor Proteins
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Transcription Factors
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hcf-1 protein, C elegans