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Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
Published on: May 10, 2018
MetWAMer: eukaryotic translation initiation site prediction
Michael E Sparks1, Volker Brendel
1Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011, USA. mespar1@iastate.edu
BMC Bioinformatics
|September 20, 2008
Summary
MetWAMer is a new software package for identifying translation initiation sites (TIS) in eukaryotic genes. Its perceptron-based model improves TIS prediction accuracy by considering start-methionine class.
Area of Science:
- Bioinformatics
- Computational Biology
- Genomics
Background:
- Accurate translation initiation site (TIS) identification is crucial for gene annotation and protein sequence delineation.
- Current methods require robust tools for processing transcript data.
- Eukaryotic TIS prediction for non-viral open reading frames is an active research area.
Purpose of the Study:
- To develop and present the MetWAMer package for TIS prediction in eukaryotic genes.
- To provide a flexible tool for post-processing gene annotations or integration into prediction pipelines.
- To improve the accuracy of TIS identification in computational genomics.
Main Methods:
- Development of the MetWAMer software package.
- Implementation of five distinct TIS prediction methods.
- Utilizing a perceptron model combining weighted signal scores and coding potential contrast.
- Incorporation of k-medoids clustering for cluster-specific parameter utilization.
Main Results:
- The perceptron-based model, combining signal scores and coding potential, achieved the highest accuracy.
- K-medoids clustering allows for tailored TIS parameter usage within specific gene clusters.
- Static weight array matrix-based indexing is effective for datasets with moderate 5'-complete coverage.
Conclusions:
- Statistically-based TIS prediction models benefit from considering start-methionine class under specific conditions.
- The perceptron-based model within MetWAMer is suitable for accurate TIS identification.
- MetWAMer is a documented, extensible, and freely available system for TIS prediction research.
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Initiation of Translation
Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
Initiation of Translation
Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...

