The major yolk protein in sea urchins is a transferrin-like, iron binding protein

被引:83
作者
Brooks, JM [1 ]
Wessel, GM [1 ]
机构
[1] Brown Univ, Dept Mol & Cell Biol, Div Biol & Med, Providence, RI 02912 USA
关键词
oogenesis; major yolk protein (MYP); yolk platelet; vitellogenin; transferrin; iron;
D O I
10.1006/dbio.2002.0611
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The major yolk protein (MYP) in sea urchins has historically been classified as a vitellogenin based on its abundance in the yolk platelets. Curiously, it is found in both sexes of sea urchins where it is presumed to play a physiological role in gametogenesis, embryogenesis, or both. Here we present the primary structure of MYP as predicted from cDNAs of two sea urchins species, Strongylocentrotus purpuratus and Lytechinus variegatus. The sequence from these two species share identity to one another, but bear no resemblance to other known vitellogenins. Instead the sequence shares identity to members of the transferrin superfamily of proteins. In vitro iron binding assays, including both Fe-39 overlay assays of MYP enriched coelomic fluid and immunoprecipitation of native iron-bound MYP from coelomic fluid, support this classification. We suggest that one of MYP's transferrin-like properties is to shuttle iron to developing germ cells. (C) 2002 Elsevier Science (USA).
引用
收藏
页码:1 / 12
页数:12
相关论文
共 59 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]   CHARACTERIZATION OF YOLK PLATELETS ISOLATED FROM DEVELOPING EMBRYOS OF ARBACIA-PUNCTULATA [J].
ARMANT, DR ;
CARSON, DD ;
DECKER, GL ;
WELPLY, JK ;
LENNARZ, WJ .
DEVELOPMENTAL BIOLOGY, 1986, 113 (02) :342-355
[3]   NEW PERSPECTIVES ON THE STRUCTURE AND FUNCTION OF TRANSFERRINS [J].
BAKER, EN ;
LINDLEY, PF .
JOURNAL OF INORGANIC BIOCHEMISTRY, 1992, 47 (3-4) :147-&
[4]   Ligand variation in the transferrin family: The crystal structure of the H249Q mutant of the human transferrin N-lobe as a model for iron binding in insect transferrins [J].
Baker, HM ;
Mason, AB ;
He, QY ;
MacGillivray, RTA ;
Baker, EN .
BIOCHEMISTRY, 2001, 40 (39) :11670-11675
[5]  
BARTFELD NS, 1990, J BIOL CHEM, V265, P21684
[6]   New perspectives on iron: An introduction [J].
Boldt, DH .
AMERICAN JOURNAL OF THE MEDICAL SCIENCES, 1999, 318 (04) :207-212
[7]  
BOWNES M, 1992, J LIPID RES, V33, P777
[8]   Transferrin in the developing ovarian follicle: evidence for de-novo expression by granulosa cells [J].
Briggs, DA ;
Sharp, DJ ;
Miller, D ;
Gosden, RG .
MOLECULAR HUMAN REPRODUCTION, 1999, 5 (12) :1107-1114
[9]   THE EVOLUTION OF EGG-YOLK PROTEINS [J].
BYRNE, BM ;
GRUBER, M ;
AB, G .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1989, 53 (01) :33-69
[10]  
CERVELLO M, 1994, EUR J CELL BIOL, V64, P314