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

• Published in: The Journal of biological chemistry Vol. 266; no. 13; pp. 8184 - 8191
• Main Authors: JUTGLAR, L, BORRELL, J. I, AUSIO, J
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 05-05-1991
• Subjects: Amino Acid Sequence; amino acids; Analytical, structural and metabolic biochemistry; Animals; biochemical analysis; Biological and medical sciences; Bivalvia; Brackish; Chromatography, Ion Exchange; DNA-Binding Proteins; electrophoresis; enzymes; Fourier Analysis; Fundamental and applied biological sciences. Psychology; histones; Histones - analysis; Histones - chemistry; Holoproteins; Male; Marine; Molecular Sequence Data; molecular weight; Mytilus californianus; Nuclear proteins; Nuclear Proteins - analysis; Nuclear Proteins - chemistry; peptides; Protein Conformation; Proteins; Sequence Homology, Nucleic Acid; spectroscopic techniques; Spectrum Analysis; sperm; spermatozoa; Spermatozoa - chemistry; Trypsin - metabolism; Ultracentrifugation; Fourier transformation; Molecular structure; Mytilus californianus; Infrared spectrometry; Trypsin; Bivalvia; Protamine; Enzymatic digestion; Isolation; Invertebrata; Mollusca; Histone H1; Nuclear protein; Aminoacid sequence
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)92959-5

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.