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Updated: Jan 26, 2026
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Molecular Evolution of the Tre Recombinase
Published on: May 29, 2008
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Increased versatility despite reduced molecular complexity: evolution, structure and function of metazoan splicing
Francesca De Bortoli1, Alexander Neumann1, Ana Kotte1
1Institut für Chemie und Biochemie, RNA Biochemie, Freie Universität Berlin, Takustr. 6, 14195 Berlin, Germany.
Nucleic Acids Research
|April 6, 2019
Summary
In metazoans, the spliceosome
Area of Science:
- Molecular Biology
- Genetics
- Structural Biology
Background:
- The Prp39/Prp42 heterodimer is crucial for spliceosome assembly in yeast.
- Metazoans lack a Prp42 ortholog, prompting investigation into functional substitution mechanisms.
Purpose of the Study:
- To elucidate the structural basis of PRPF39 function in metazoans.
- To understand the evolutionary adaptation of spliceosome components.
Main Methods:
- X-ray crystallography to determine the structure of murine PRPF39.
- Site-directed mutagenesis to assess the role of PRPF39 homodimerization.
- Phylogenetic analysis of U1 snRNA and spliceosomal proteins.
Main Results:
- Murine PRPF39 forms a functional homodimer, unlike the yeast heterodimer.
- Disruption of PRPF39 homodimerization impairs splicing.
- PRPF39 expression is regulated by NMD-inducing alternative splicing.
- Phylogenetic analysis reveals coevolution between U1 snRNA length and Prp42 absence.
Conclusions:
- The PRPF39 homodimer functionally replaces the Prp39/Prp42 heterodimer in metazoans.
- Splicing complexity correlates with the substitution of the heterodimer with a homodimer.
- PRPF39 homodimerization is essential for efficient splicing and adaptation to cellular requirements.
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