AMINO-ACID-SEQUENCE OF THE HUMAN INTERMEDIATE BASIC-PROTEIN 2 (HPI2) FROM SPERM NUCLEI - STRUCTURAL RELATIONSHIP WITH PROTAMINE-P2

Citation
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
Citations number
28
Categorie Soggetti
Biology
ISSN journal
00142956
Volume
214
Issue
2
Year of publication
1993
Pages
445 - 450
Database
ISI
SICI code
0014-2956(1993)214:2<445:AOTHIB>2.0.ZU;2-H
Abstract
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.