PL-I of Spisula solidissima, a Highly Elongated Sperm-Specific Histone H1
| Autor: | John D. Lewis, Reginald McParland, Juan Ausió |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Male
Molecular Sequence Data Biochemistry Mass Spectrometry Histones Complete sequence Surf clam Histone H1 Animals Amino Acid Sequence 3' Untranslated Regions Gene DNA Primers chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid biology biology.organism_classification Spermatozoa Molecular biology Protein tertiary structure Bivalvia Amino acid Histone chemistry biology.protein Spisula Protein Binding |
| Zdroj: | Biochemistry. 43:7766-7775 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi0360455 |
| Popis: | The major chromosomal protein of the mature sperm of the surf clam, Spisula solidissima ,i s a histone H1-related protamine-like (PL-I) protein of low electrophoretic mobility. We report here the complete sequence of two isoforms of its encoding genes. These genes encode a protein of 453 and 454 amino acids, respectively. The predicted mass of the larger isoforms (51 437 Da) was confirmed using electrospray ionization mass spectrometry. The amino-terminal tail of the S. solidissima PL-I is greatly elongated because of the presence of 39 tandem hexapeptide repeats of the motif (K/R)KRSAS with a few semiconservative amino acid substitutions. These repeats are very closely mirrored by their encoding DNA sequence, which indicates that an expansion because of sequence duplication most likely occurred. The C-terminal domain consists of a histone H1-related core with a predicted winged-helix tertiary structure, which is followed by an unstructured lysine-rich tail. This information provides additional molecular support for the classification and underlying evolution of sperm nuclear basic proteins in bivalve molluscs. |
| Databáze: | OpenAIRE |
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