Function of RRM domains of Drosophila melanogaster ELAV: Rnp1 mutations and rrm domain replacements with ELAV family proteins and SXL
| Autor: | Kalpana White, Marshall Gordon, Yvonne M. Yannoni, Michael J. Lisbin |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Ribosomal Proteins
Saccharomyces cerevisiae Proteins Ribonucleoside Diphosphate Reductase Amino Acid Motifs Immunoblotting Molecular Sequence Data RNA-binding protein Nerve Tissue Proteins medicine.disease_cause Polymerase Chain Reaction Protein Structure Secondary Mutant protein Genetics medicine Melanogaster Animals Drosophila Proteins Amino Acid Sequence Transgenes Amino Acids Ribonucleoprotein Mutation biology Sequence Homology Amino Acid Tumor Suppressor Proteins Genetic Complementation Test RNA-Binding Proteins Sequence Analysis DNA biology.organism_classification Immunohistochemistry Protein Structure Tertiary Drosophila melanogaster ELAV Proteins Ribonucleoproteins Mutagenesis Insect Hormones RNA Nuclear localization sequence Drosophila Protein Plasmids Research Article |
| Zdroj: | Genetics. 155(4) |
| ISSN: | 0016-6731 |
| Popis: | Members of the ELAV family of proteins contain three RNA recognition motifs (RRMs), which are highly conserved. ELAV, a Drosophila melanogaster member of this family, provides a vital function and exhibits a predominantly nuclear localization. To investigate if the RNA-binding property of each of the ELAV RRMs is required for ELAV's in vivo function, amino acid residues critical in RNA binding for each RRM were individually mutated. A stringent genetic complementation test revealed that when the mutant protein was the sole source of ELAV, RNA-binding ability of each RRM was essential to ELAV function. To assess the degree to which each domain was specific for ELAV function and which domains perhaps performed a function common to related ELAV proteins, we substituted an ELAV RRM with the corresponding RRM from RBP9, the D. melanogaster protein most homologous to ELAV; HuD, a human ELAV family protein; and SXL, which, although evolutionarily related, is not an ELAV family member. This analysis revealed that RRM3 replacements were fully functional, but RRM1 and RRM2 replacements were largely nonfunctional. Under less stringent conditions RRM1 and RRM2 replacements from SXL and RRM1 replacement from RBP9 were able to provide supplemental function in the presence of a mutant hypomorphic ELAV protein. |
| Databáze: | OpenAIRE |
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