E. Alimi et al., AMINO-ACID-SEQUENCE OF THE HUMAN INTERMEDIATE BASIC-PROTEIN 2 (HPI2) FROM SPERM NUCLEI - STRUCTURAL RELATIONSHIP WITH PROTAMINE-P2, European journal of biochemistry, 214(2), 1993, pp. 445-450
Human intermediate basic protein 2 (HPI2) is a low-molecular-mass basi
c protein present in small amounts in human sperm nuclei. The amino ac
id composition of the protein, its N-terminal amino acid sequence and
peptide maps obtained after digestion with endoproteinases Lys-C and G
lu-C, reveal that HPI2 is structurally related to human protamine spec
ies P2 (HP2), which is rich in Arg, His and Cys residues. Compared to
HP2, which is one of the two major sperm protamines, HPI2 has an N-ter
minal extension of 24 residues which includes six acidic residues and
does not possess any Arg residues. The amino acid sequence of HPI2 (81
residues) is identical to the sequence of the C-terminal region of an
other minor sperm nuclear protein, human intermediate basic protein 1
(HPI1, 101 residues), which was sequenced previously [Martinage, A., A
rkhis, A., Alimi, E., Sautiere, P. & Chevaillier, P. (1990) Eur. J. Bi
ochem. 191, 449-451]. Due to this structural similarity, HPI2 must be
considered as an intermediate in the maturation of proprotamine HPI1 l
imited proteolysis.