Primary, secondary, and tertiary structure of the core of a histone H1-like protein from the sperm of Mytilus

L. Jutglar, J. I. Borrell, J. Ausio

Research output: Indexed journal article Articlepeer-review

37 Citations (Scopus)

Abstract

We have analyzed the structure of the trypsin-resistant core of the protein PL-II* of the sperm from Mytilus californianus. The peptide has a molecular mass of 8436 Da and its primary sequence is ATGGAKKP STLSMIVAAIQAMKNRKGSSVQAIRKYILANNKG INTSRLGSAMKLAFAKGLKSGVLVRPKTSAGA SGATGSFRVG. This sequence bears an enormous homology and fulfills the constraints of the consensus sequence of the trypsin-resistant peptides of the proteins of the histone H1 family. Secondary structure analysis using Fourier-transform infrared spectroscopy as well as predictive methods indicate the presence of 20-30% β-structure and ~25% α-helix for this peptide. As in the case of histone H1 proteins, the protein PL-II* core exhibits a compact globular structure as deduced from hydrodynamic measurements. The presence of a histone H1 protein with protamine-like features, seems to be thus, a common general feature of the chromatin composition in the sperm of the bivalve molluscs.

Original languageEnglish
Pages (from-to)8184-8191
Number of pages8
JournalJournal of Biological Chemistry
Volume266
Issue number13
Publication statusPublished - 1991
Externally publishedYes

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