Primary structure of scombrine α:: Two different species with an identical protamine

被引:3
作者
Buesa, C
del Valle, L
Saperas, N
Goethals, M
Lloris, D
Chiva, M
机构
[1] State Univ Ghent VIB, Fac Med, Dept Biochem, B-9000 Ghent, Belgium
[2] UPC, ETSEIB, Dept Engn Quim, Barcelona 08028, Spain
[3] CSIC, Inst Ciencias Mar, E-08039 Barcelona, Spain
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1998年 / 119卷 / 01期
关键词
sperm specific protein; nuclear protein; protamine; primary structure; protein evolution; sperm; fish; Scomber;
D O I
10.1016/S0305-0491(97)00297-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have studied the protamine scombrine alpha from the mackerel Scomber scombrus. Scombrine alpha is found phosphorylated in spermatid nuclei, but not in nuclei of ripe sperm. It is a typical fish protamine, made up of two distinct molecular species, each of 34 amino acid residues. The primary structure of the main component of scombrine alpha is 100% identical to scombrine gamma, the nonmicroheterogeneous protamine from Scomber australasicus (11). The second component of scombrine alpha is a very minor molecular species that has an isoleucine instead of a valine in position 11. Nuclear sperm-specific basic proteins display an enormous interspecific variability and it is very surprising that two different species show identical protamines. In this work eve suggest that evolutionary changes in primary structure of protamines are restricted by several constitutive factors, especially when protamines either lack or have a low degree of microheterogeneity. (C) 1998 Elsevier Science Inc.
引用
收藏
页码:145 / 149
页数:5
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