title: Role of structural flexibility in the evolution of emerin.
abstract: Emerin is a short inner nuclear membrane protein with an LEM-domain at the N-terminal end and a transmembrane domain at the C-terminal end. The middle region of human emerin contains multiple binding motifs. Since emerin is often found in evolutionarily newer species, the functional conservation of emerin becomes an interesting topic. In this study, we have demonstrated that most of the functional motifs of emerin are intrinsically disordered or highly flexible. Many post-translational modification sites and mutation sites are associated with these disordered regions. The averaged substitution rates of most functional motifs between species correlate positively with the averaged disorder scores of those functional motifs. Human emerin sequence may have acquired new functions on protein-protein interaction through the formation of hydrophobic motifs in the middle region, which is resulted from accumulated mutations during the evolution process.
authors: Department of Cell Biology, Microbiology and Molecular Biology, School of Natural Sciences and Mathematics, College of Arts and Sciences, University of South Florida, 4202 E. Fowler Ave, ISA 2015, Tampa, FL 33620, USA.
authors: Jia
authors: J
authors: Yuan
authors: Department of Cell Biology, Microbiology and Molecular Biology, School of Natural Sciences and Mathematics, College of Arts and Sciences, University of South Florida, 4202 E. Fowler Ave, ISA 2015, Tampa, FL 33620, USA. Electronic address: binxue@usf.edu.
authors: Bin
authors: B
authors: Xue
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D030562:Databases, Protein; D019143:Evolution, Molecular; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D064267:Intrinsically Disordered Proteins / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics*; D010802:Phylogeny; D021281:Quantitative Structure-Activity Relationship; D016415:Sequence Alignment
chemical_list: D064267:Intrinsically Disordered Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins; C092710:emerin
keywords: EMD; Intrinsic disorder; Mutation; Phylogenetic analysis; Substitution