Alternative splicing and protein structure evolution.

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Alternative splicing and protein structure evolution. Abstract Text:

Fabian Birzele,Gergely Csaba,Ralf Zimmer,

Alternative splicing is thought to be one of the major sources for functional diversity in higher eukaryotes. Interestingly, when mapping splicing events onto protein structures, about half of the events affect structured and even highly conserved regions i.e. are non-trivial on the structure level. This has led to the controversial hypothesis that such splice variants result in nonsense-mediated mRNA decay or non-functional, unstructured proteins, which do not contribute to the functional diversity of an organism. Here we show in a comprehensive study on alternative splicing that proteins appear to be much more tolerant to structural deletions, insertions and replacements than previously thought. We find literature evidence that such non-trivial splicing isoforms exhibit different functional properties compared to their native counterparts and allow for interesting regulatory patterns on the protein network level. We provide examples that splicing events may represent transitions between different folds in the protein sequence-structure space and explain these links by a common genetic mechanism. Taken together, those findings hint to a more prominent role of splicing in protein structure evolution and to a different view of phenotypic plasticity of protein structures.

Alternative splicing and protein structure evolution. Publishing Authors By Initials

F Birzele,G Csaba,R Zimmer,

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Alternative splicing and protein structure evolution. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Nucleic acids research

VOLUME: 36

Page Numbers: 550-8

Journal Abbreviation: Nucleic Acids Res.

ISSN: 1362-4962

DAY: 30

MONTH: 11

YEAR: 2007

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LANGUAGE: eng

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Grant and Affiliation Information for Alternative splicing and protein structure evolution.

AFFILIATION: Practical Informatics and Bioinformatics Group, Department of Informatics, Ludwig-Maximilians-University, Amalienstrasse 17, D-80333 Munich, Germany. fabian.birzele@bio.ifi.lmu.de

Country: England

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MEDLINETA: Nucleic Acids Res

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