title: Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex.
abstract: The CCR4 protein from Saccharomyces cerevisiae is a component of a multisubunit complex that is required for the regulation of a number of genes in yeast cells. We report here the identification of a mouse protein (mCAF1 [mouse CCR4-associated factor 1]) which is capable of interacting with and binding to the yeast CCR4 protein. The mCAF1 protein was shown to have significant similarity to proteins from humans, Caenorhabditis elegans, Arabidopsis thaliana, and S. cerevisiae. The yeast gene (yCAF1) had been previously cloned as the POP2 gene, which is required for expression of several genes. Both yCAF1 (POP2) and the C. elegans homolog of CAF1 were shown to genetically interact with CCR4 in vivo, and yCAF1 (POP2) physically associated with CCR4. Disruption of the CAF1 (POP2) gene in yeast cells gave phenotypes and defects in transcription similar to those observed with disruptions of CCR4, including the ability to suppress spt10-enhanced ADH2 expression. In addition, yCAF1 (POP2) when fused to LexA was capable of activating transcription. mCAF1 could also activate transcription when fused to LexA and could functionally substitute for yCAF1 in allowing ADH2 expression in an spt10 mutant background. These data imply that CAF1 is a component of the CCR4 protein complex and that this complex has retained evolutionarily conserved functions important to eukaryotic transcription.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of New Hampshire, Durham 03824, USA.
authors.forename: M P
authors.initials: MP
authors.lastname: Draper
authors.forename: C
authors.initials: C
authors.lastname: Salvadore
authors.forename: C L
authors.initials: CL
authors.lastname: Denis
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D029681:Arabidopsis Proteins; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D005057:Eukaryotic Cells / Q000502:physiology; D005095:Exoribonucleases; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D007930:Leucine / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011485:Protein Binding; D011506:Proteins; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid; D012097:Repressor Proteins; D012260:Ribonucleases; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases; D013045:Species Specificity; D013329:Structure-Activity Relationship; D000637:Transaminases; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism*; D014158:Transcription, Genetic; D000099160:LexA Repressor Protein
chemical_list: D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D005095:Exoribonucleases; D005656:Fungal Proteins; D007930:Leucine; D011506:Proteins; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D012260:Ribonucleases; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases; D000637:Transaminases; D014157:Transcription Factors; D000099160:LexA Repressor Protein; C489779:POP2 protein, Arabidopsis; C078657:CCR4 protein, S cerevisiae; C489778:Cnot7 protein, mouse; C079009:POP2 protein, S cerevisiae