Insect Molecular Biology · 1996 · 58 citations · 21 references
Life SciencesBiologyMolecular BiologyComparative GenomicsGenomicsInsect GeneticsProtein StructureRibosome FunctionTranslation In EukaryotesTranslation In ProkaryotesConserved Region AnalysisMolecular Mass DeterminationPrimary Rna StructureRibosomal Protein StructureRibosomal Rna Sequence ConservationRibosomal Rna Structural ConstraintsRibosomal Rna-protein InteractionsRibosomal Rnas
We have isolated from Manduca sexta full-length cDNAs encoding proteins homologous to human ribosomal proteins S3 and S7. These are the first ribosomal protein sequences obtained from non-Dipteran insects. M. sexta ribosomal protein S3 has a molecular mass of 26,715 Da. Ribosomal protein S7 has a mass 21,870 Da. Both are basic proteins, with abundant Lys and Arg residues that may interact with ribosomal RNA in the ribosome. Southern blot hybridization suggests the presence of single genes for both ribosomal proteins in the M. sexta genome. Alignments with other S3 and S7 sequences available In the database indicate regions of the ribosomal proteins that have been the most highly conserved in evolution and may point to important functional regions in the proteins. Ribosomal protein S3 appears to be more highly conserved then ribosomal protein S7. This may be due to greater constraints on the structure of S3 because of its dual functions in translation as a ribosomal protein and in DNA repair in the nucleus.
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Basic local alignment search tool
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