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Protamine-like Proteins in 12 Sequenced Species of Drosophila

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The current study was aimed at analyzing putative protein sequences of the protamine-like proteins of 12 Drosophila species based on the reference sequences of two protamine-like proteins (Mst35Ba and Mst35Bb) found in Drosophila melanogaster sperm nuclei. Protamine-like proteins belong to a larger group of proteins that are involved in DNAbinding known as sperm nuclear basic proteins (SNBPs). SNBPs play a role in chromatin condensation during the postmeiotic stage of spermatogenesis, termed spermiogenesis. During spermiogenesis, nuclear transformation occurs where histones are exchanged for SNBPs, the chromatin condenses, and the nucleus transforms into a needle-like shape in Drosophila. Our goal was to search the 12 sequenced Drosophila genomes for protamine-like proteins based on the known sequences for D. melanogaster. Searches were performed on genomic DNA, mRNA transcripts and amino acid sequences using NCBI basic local alignment search tool (BLAST). Sequence alignments and analysis of amino acid content indicate that homologs for Mst35Ba and Mst35Bb are present in all 12 species of flies analyzed in this study. Functional analyses of a conserved region found within the proteins indicate the presence of a DNA-binding domain, possibly a high mobility group DNA- binding box. This study represents the first large-scale, single-genus dataset for protamine-like proteins and provides the basis for a fine-grained analysis of their evolution.
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Keywords: Chromatin; DNA- binding box; Drosophila; SNBP; chromatin condensation; protamine-like protein; protamines; protein sequences; sperm nuclear basic proteins; spermatogenesis

Document Type: Research Article

Publication date: 2013-01-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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