Literature DB >> 17476531

Coiled coil structures and transcription: an analysis of the S. cerevisiae coilome.

Kellie E Barbara1, Kristine A Willis, Terry M Haley, Stephen J Deminoff, George M Santangelo.   

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.

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Year:  2007        PMID: 17476531     DOI: 10.1007/s00438-007-0237-x

Source DB:  PubMed          Journal:  Mol Genet Genomics        ISSN: 1617-4623            Impact factor:   2.980


  85 in total

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5.  Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence.

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6.  Predicting coiled coils by use of pairwise residue correlations.

Authors:  B Berger; D B Wilson; E Wolf; T Tonchev; M Milla; P S Kim
Journal:  Proc Natl Acad Sci U S A       Date:  1995-08-29       Impact factor: 11.205

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5.  Reversible pH-controlled DNA-binding peptide nanotweezers: an in-silico study.

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6.  The fungus Ustilago maydis and humans share disease-related proteins that are not found in Saccharomyces cerevisiae.

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7.  Protein-Protein Interactions Mediated by Helical Tertiary Structure Motifs.

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