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The ITS2 Database
Published on: March 12, 2012
SECISaln, a web-based tool for the creation of structure-based alignments of eukaryotic SECIS elements
Charles E Chapple1, Roderic Guigó, Alain Krol
1Institut Municipal d'Investigació Mèdica, Universitat Pompeu Fabra and Parc de Recerca Biomedica de Barcelona, Carrer del Doctor Aiguader 88, 08003, Barcelona, Catalonia, Spain. charles.chapple@crg.es
Bioinformatics (Oxford, England)
|January 31, 2009
Summary
A new tool called SECISaln enables the alignment of SECIS elements, crucial for selenoprotein production. This advancement aids in understanding SECIS structure and identifying conserved sequences in selenoprotein messenger RNAs.
Area of Science:
- Molecular Biology
- Genomics
- Bioinformatics
Background:
- Selenoproteins incorporate the 21st amino acid, selenocysteine, via a UGA codon recoding mechanism.
- This recoding relies on a specific RNA structure, the SECIS element, in the 3' untranslated region of selenoprotein mRNAs.
- Previous limitations in sequence data hindered comprehensive analysis of SECIS element conservation.
Purpose of the Study:
- To develop a tool for structure-based sequence alignment of SECIS elements.
- To enhance the understanding of SECIS secondary structure and identify conserved nucleotide positions.
- To provide a valuable resource for researchers in the selenoprotein and RNA fields.
Main Methods:
- Development of the web-based tool SECISaln.
- Utilizing the defined secondary structure of SECIS RNA for alignment.
- Leveraging an expanded dataset of eukaryotic selenoprotein mRNA sequences.
Main Results:
- SECISaln provides the first extensive, structure-based sequence alignment of SECIS elements.
- The tool facilitates improved knowledge of SECIS secondary structure.
- Novel conserved nucleotide positions within SECIS elements have been identified.
Conclusions:
- SECISaln is a powerful new tool for the selenoprotein and RNA research communities.
- The tool aids in the discovery of conserved elements within SECIS structures.
- This work advances the study of selenoprotein biosynthesis and regulation.

