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The relationship between coding sequences and function in some heme binding proteins
Journal of Molecular Evolution
|December 1, 1980
Insights
Globin genes have three exons, with the middle one crucial for heme binding. This structure
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Globin genes possess three exons, with the central exon encoding a four-helical structure vital for heme binding.
- This globin peptide chain structure is structurally similar to cytochrome c and cytochrome b5.
Purpose of the Study:
- To infer the exon-intron structure of cytochrome c and cytochrome b5 genes based on structural similarities with globin genes.
Main Methods:
- Comparative analysis of protein structures.
- Inference of gene structure based on conserved functional domains.
Main Results:
- The cytochrome c gene is predicted to have a single coding sequence.
- The cytochrome b5 gene is predicted to have three exons, similar to the globin gene.
Conclusions:
- Gene structure can be inferred from conserved protein supersecondary structures.
- Evolutionary relationships between heme-binding proteins may be reflected in their gene organization.
Abstract:
It is known that globin genes contain three exons with the middle exon coding for a four-helical supersecondary structure responsible for heme binding. Since this portion of the globin peptide chain can be structurally superimposed onto the cytochrome c and cytochrome b5 chains (Argos and Rossmann 1979), it can be inferred that the cytochrome c gene will contain only one coding sequence while the cytochrome b5 gene will be composed of three exons as found in the globin gene.