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 infared spectroscopy as well as predictive methods indicate the presence of 20-30% beta-structure and approximately 25% alpha-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.
Highlights
We have analyzed the structure of the trypsin-resist- many years, a true sperm-specific histone H2B (Ausio and ant core of the protein PL-11* of the sperm from M y - Subirana, 1982).its electrophoretic mobility in tilus californianus
One of the most significant featuroefsthe proteinmembers of the histone H1 family is the presenceof a folded trypsinresistant internal core (Allan et al, 1980) which is the ence of a histone H 1 protein with protamine-like fea- more evolutionarily conserved region of the molecule (Cole, tures, seems to be a common general feature of 1987).This region usually contains 82 k 4 amino acids and is the chromatin composition in the sperm ofthe bivalve organized in aglobular structure which results from the molluscs
These proteins can be fractionated in one step, usingionic exchangechromatography (Ausio, 1986).The protein PL-11* wasisolatedin this way (Fig. IC) and was further digested with trypsin toyield a trypsin-resistant peptide (Fig. 1B).The time course of digestion is shown in Fig
Summary
We have analyzed the structure of the trypsin-resist- many years, a true sperm-specific histone H2B (Ausio and ant core of the protein PL-11* of the sperm from M y - Subirana, 1982).its electrophoretic mobility in tilus californianus. This sequence bears an enormousho- 11*and have identified it with the members of the histoneH1 mology and fulfills the constraints of the consensus sequence of the trypsin-resistant peptides of the proteins of the histone H1 family. One of the most significant featuroefsthe proteinmembers of the histone H1 family is the presenceof a folded trypsinresistant internal core (Allan et al, 1980) which is the ence of a histone H 1 protein with protamine-like fea- more evolutionarily conserved region of the molecule (Cole, tures, seems to be a common general feature of 1987).This region usually contains 82 k 4 amino acids and is the chromatin composition in the sperm ofthe bivalve organized in aglobular structure which results from the molluscs
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
