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Histone H1‐like protein and a testis‐specific variant in the reproductive tracts of Octopus vulgaris
Author(s) -
Mennella Maria Rosaria Faraone,
Farina Benedetta,
Irace Maria Venezia,
Cristo Carlo Di,
Cosmo Anna Di
Publication year - 2002
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.90020
Subject(s) - biology , circular dichroism , octopus (software) , histone h1 , histone , dna , biochemistry , nucleic acid , amino acid , microbiology and biotechnology , prostatic acid phosphatase , enzyme , acid phosphatase , physics , quantum mechanics
In this study, we have identified a 28‐kDa protein resembling the linker H1 in the testis and prostate of the reproductive system of Octopus vulgaris . This protein, Ov H1, was partially purified by reverse phase high‐pressure liquid chromatography (HPLC) of the perchloric acid extract from testis nuclei. It showed electrophoretic mobility, CD spectrum and amino acid composition highly comparable with those of the mammalian histone. Moreover, it was microheterogeneous, as resulted from prostate and testis HPLC and mass spectrometry analyses. Such analysis showed that in testis there are two H1 subfractions, which do not appear in the prostate. Amino acid composition of the major testis specific variant ( Ov H1t) showed high similarity with rat testis specific H1t. The histone‐like nature of Ov H1 was confirmed by its ability to bind DNA as tested both by circular dichroism and protection of the nucleic acid toward deoxyribonuclease I activity. The circular dichroism spectra of Octopus DNA in the absence and presence of increasing amounts of the protein showed a dose‐dependent effect, leading to a progressive compactness of the polynucleotide. Ov H1/DNA complexes were also resistant to nuclease digestion. The presence of H1 in the testis and prostate of the reproductive system of Octopus is discussed in light of the fact that there is a similarity between its behavior and that of vertebrates. Mol. Reprod. Dev. 63: 355–365, 2002. © 2002 Wiley‐Liss, Inc.