title: Coiled coil structures and transcription: an analysis of the S. cerevisiae coilome.
abstract: The alpha-helical coiled coil is a simple but widespread motif that is an integral feature of many cellular structures. Coiled coils allow monomeric building blocks to form complex assemblages that can serve as molecular motors and springs. Previous parametrically delimited analyses of the distribution of coiled coils in the genomes of diverse organisms, including Escherichia coli, Saccharomyces cerevisiae, Arabidopsis thaliana, Caenorhabditis elegans and Homo sapiens, have identified conserved biological processes that make use of this versatile motif. Here we present a comprehensive inventory of the set of coiled coil proteins in S. cerevisiae by combining multiple coiled coil prediction algorithms with extensive literature curation. Our analysis of this set of proteins, which we call the coilome, reveals a wider role for this motif in transcription than was anticipated, particularly with respect to the category that includes nucleocytoplasmic shuttling factors involved in transcriptional regulation. We also show that the constitutively nuclear yeast transcription factor Gcr1 is homologous to the mammalian transcription factor MLL3, and that two coiled coil domains conserved between these homologs are important for Gcr1 dimerization and function. These data support the hypothesis that coiled coils are required to assemble structures essential for proper functioning of the transcriptional machinery.
authors.affiliation: Mississippi Functional Genomics Network, The University of Southern Mississippi, Hattiesburg, MS, USA.
authors.forename: Kellie E
authors.initials: KE
authors.lastname: Barbara
authors.forename: Kristine A
authors.initials: KA
authors.lastname: Willis
authors.forename: Terry M
authors.initials: TM
authors.lastname: Haley
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Deminoff
authors.forename: George M
authors.initials: GM
authors.lastname: Santangelo
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry*; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D014157:Transcription Factors; D014158:Transcription, Genetic
chemical_list: D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C076227:GCR1 protein, S cerevisiae; C452979:KMT2C protein, human; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D011495:Histone-Lysine N-Methyltransferase; C510652:Kmt2c protein, mouse