Co-evolution of the branch site and SR proteins in eukaryotes

Serine–arginine-rich (SR) proteins are essential for splicing in metazoans but are absent in yeast. By contrast, many fungi have SR protein homologs with variable arginine-rich regions analogous to the arginine–serine-rich (RS) domain in metazoans. The density of RS repeats in these regions correlat...

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Published inTrends in genetics Vol. 24; no. 12; pp. 590 - 594
Main Authors Plass, Mireya, Agirre, Eneritz, Reyes, Diana, Camara, Francisco, Eyras, Eduardo
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Ltd 01.12.2008
Cambridge, UK: Elsevier Trends Journals
Elsevier
Subjects
Animalia
Biological and medical sciences
Biological evolution
coevolution
eukaryotic cells
Eukaryotic Cells - metabolism
Evolution, Molecular
Exons - genetics
Fundamental and applied biological sciences. Psychology
Genetics of eukaryotes. Biological and molecular evolution
Medical Education
Metazoa
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nucleic Acid Conformation
Protein Binding
Protein Structure, Tertiary
proteins
RNA Splicing
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
Serine-Arginine Splicing Factors
yeasts
Eukaryote
Molecular evolution
Genetics
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Summary:Serine–arginine-rich (SR) proteins are essential for splicing in metazoans but are absent in yeast. By contrast, many fungi have SR protein homologs with variable arginine-rich regions analogous to the arginine–serine-rich (RS) domain in metazoans. The density of RS repeats in these regions correlates with the conservation of the branch site signal, providing evidence for an ancestral origin of SR proteins and indicating that the SR proteins and the branch site co-evolved.
Bibliography:http://dx.doi.org/10.1016/j.tig.2008.10.004
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ISSN:0168-9525
DOI:10.1016/j.tig.2008.10.004