Nowa, a novel protein with minicollagen Cys-rich domains, is involved in nematocyst formation in Hydra

被引:61
作者
Engel, U
Oezbek, S
Engel, R
Petri, B
Lottspeich, F
Holstein, TW [1 ]
机构
[1] Tech Univ Darmstadt, Inst Zool, D-64287 Darmstadt, Germany
[2] Univ Basel, Biozentrum, Dept Biophys Chem, CH-4056 Basel, Switzerland
[3] Univ Munich, Inst Zool, D-80333 Munich, Germany
[4] Max Planck Inst Biochem, D-82152 Martinsried, Germany
关键词
minicollagen Cys-rich domain; CTLD; nematocyst; microtubules; assembly;
D O I
10.1242/jcs.00084
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The novel protein Nowa was identified in nematocysts, explosive organelles of Hydra, jellyfish, corals and other Cnidaria. Biogenesis of these organelles is complex and involves assembly of proteins inside a post-Golgi vesicle to form a double-layered capsule with a long tubule. Nowa is the major component of the outer wall, which is formed very early in morphogenesis. The high molecular weight glycoprotein has a modular structure with an N-terminal sperm coating glycoprotein domain, a central C-type lectin-like domain, and an eightfold repeated cysteine-rich domain at the C-terminus. Interestingly, the cysteine-rich domains are homologous to the cysteine-rich domains of minicollagens. We have previously shown that the cysteines of these minicollagen cysteine-rich domains undergo an isomerization process from intra- to intermolecular disulfide bonds, which mediates the crosslinking of minicollagens to networks in the inner wall of the capsule. The minicollagen cysteine-rich domains present in both proteins provide a potential link between Nowa in the outer wall and minicollagens in the inner wall. We propose a model for nematocyst formation that integrates cytoskeleton rearrangements around the post-Golgi vesicle and protein assembly inside the vesicle to generate a complex structure that is stabilized by intermolecular disulfide bonds.
引用
收藏
页码:3923 / 3934
页数:12
相关论文
共 35 条
[1]   A common motif in proparts of Cnidarian toxins and nematocyst collagens and its putative role [J].
Anderluh, G ;
Podlesek, Z ;
Macek, P .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 2000, 1476 (02) :372-376
[2]  
DAVID CN, 1974, J CELL SCI, V16, P359
[3]   QUANTITATIVE METHOD FOR MACERATION OF HYDRA TISSUE [J].
DAVID, CN .
WILHELM ROUX ARCHIV FUR ENTWICKLUNGSMECHANIK DER ORGANISMEN, 1973, 171 (04) :259-268
[4]  
DAVID CN, 1974, AM ZOOL, V14, P537
[5]  
DRICKAMER K, 1988, J BIOL CHEM, V263, P9557
[6]   C-type lectin-like domains [J].
Drickamer, K .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1999, 9 (05) :585-590
[7]  
Drickamer K., 1989, Ciba Foundation Symposium, P45
[8]   INTERNAL AMINO-ACID SEQUENCE-ANALYSIS OF PROTEINS SEPARATED BY GEL-ELECTROPHORESIS AFTER TRYPTIC DIGESTION IN POLYACRYLAMIDE MATRIX [J].
ECKERSKORN, C ;
LOTTSPEICH, F .
CHROMATOGRAPHIA, 1989, 28 (1-2) :92-94
[9]   A switch in disulfide linkage during minicollagen assembly in Hydra nematocysts [J].
Engel, U ;
Pertz, O ;
Fauser, C ;
Engel, J ;
David, CN ;
Holstein, TW .
EMBO JOURNAL, 2001, 20 (12) :3063-3073
[10]  
Frohman Michael A., 1995, P381