Alternative splicing in human transcriptome: Functional and structural influence on proteins
| Autor: | Kei Hagino, Yoshinori Hirashima, Tatsuya Eguchi, Taku Nakahara, Kazuki Shinoda, Atsushi Hijikata, Mitiko Go, Takeshi Itoh, Ken ichi Takahashi, Akihiro Yamaguchi, Kei Yura, Tadashi Imanishi, Takashi Gojobori, Masafumi Shionyu |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein isoform Gene isoform DNA Complementary Proteome Transcription Genetic Protein Conformation Molecular Sequence Data Protein domain Biology Models Biological Receptors G-Protein-Coupled Protein structure GTP-Binding Proteins Protein splicing Protein Interaction Mapping Genetics Humans Protein Isoforms Amino Acid Sequence RNA Messenger Gene Apelin Receptors NAB2 Alternative splicing Computational Biology General Medicine Protein Structure Tertiary Cell biology Alternative Splicing RNA Helicases Protein Binding Signal Transduction |
| Zdroj: | Gene. 380:63-71 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/j.gene.2006.05.015 |
| Popis: | Alternative splicing is a molecular mechanism that produces multiple proteins from a single gene, and is thought to produce variety in proteins translated from a limited number of genes. Here we analyzed how alternative splicing produced variety in protein structure and function, by using human full-length cDNAs on the assumption that all of the alternatively spliced mRNAs were translated to proteins. We found that the length of alternatively spliced amino acid sequences, in most cases, fell into a size shorter than that of average protein domain. We evaluated comprehensively the presumptive three-dimensional structures of the alternatively spliced products to assess the impact of alternative splicing on gene function. We found that more than half of the products encoded proteins which were involved in signal transduction, transcription and translation, and more than half of alternatively spliced regions comprised interaction sites between proteins and their binding partners, including substrates, DNA/RNA, and other proteins. Intriguingly, 67% of the alternatively spliced isoforms showed significant alterations to regions of the protein structural core, which likely resulted in large conformational change. Based on those findings, we speculate that there are a large number of cases that alternative splicing modulates protein networks through significant alteration in protein conformation. |
| Databáze: | OpenAIRE |
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