6533b858fe1ef96bd12b58d6
RESEARCH PRODUCT
Polymorphism of mytilin B mRNA is not traslated into mature peptide
Maria Giovanna ParisiMylène ToubianaHui LiMatteo CammarataPhilippe RochNicolò Parrinellosubject
ImmunologyMolecular Sequence DataAntimicrobial peptide Defensin mRNA polymorphism DGGE.Evolution MolecularExonchemistry.chemical_compoundOpen Reading FramesAnimalsAmino Acid SequenceRNA MessengerSelection GeneticMolecular BiologyGenePeptide sequencePhylogenyGeneticsElectrophoresis Agar GelMytilusGenomePolymorphism GeneticbiologyBase SequenceMytilinNucleic acid sequenceIntronExonsbiology.organism_classificationMolecular biologyMytiluschemistryGene Expression RegulationProtein BiosynthesisPeptidesTemperature gradient gel electrophoresisAntimicrobial Cationic Peptidesdescription
Diversity of mRNAs from mytilin B, one of the five mytilins identified in the Mediterranean mussel, Mytilus galloprovincialis, has been investigated from circulating hemocytes. One mussel expressed simultaneously two to ten different mytilin B mRNAs as observed in denaturing gradient gel electrophoresis (DGGE), defining 10 individual DGGE patterns (named A to J) within the mussels from Messina, Sicily (Italy). Three patterns accounted for 79% of the individuals whereas other patterns were found in only 2-7% of the 57 analyzed mussels. Base mutations were observed at specific locations, mainly within COOH-terminus and 3'UTR, leading to 36 nucleotide sequence variants and 21 different coding sequences (cds) segregating in two different clusters. Most of the base mutations were silent, and the number of pro-peptide variants was restricted to four. Finally, as the two amino acid replacements occurred within COOH-terminus, mature peptide from mytilin B appeared unique. Multiple sequencing of partial mytilin B gene from one mussel revealed that one to four randomly distributed mutation points occurred within intron-3. Only one sequence out of the 91 analyzed contained 16 mutation points. In addition, this sequence was the only one containing four out of the six mutation points occurring within exon-4, that code for most of the COOH-terminus domain, including the unique amino acid replacement. Statistical tests for neutrality indicated negative selection pressure on signal and mature peptide domains, but possible positive selection pressure for COOH-terminus domain.
year | journal | country | edition | language |
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2008-10-02 |