Kurz E M, Holstein T W, Petri B M, Engel J, David C N
Department of Zoology, University of Munich, Germany.
J Cell Biol. 1991 Nov;115(4):1159-69. doi: 10.1083/jcb.115.4.1159.
We have isolated and characterized four collagen-related c-DNA clones (N-COL 1, N-COL 2, N-COL 3, N-COL 4) that are highly expressed in developing nematocytes in hydra. All four c-DNAs as well as their corresponding transcripts are small in size (600-1,000 bp). The deduced amino acid sequences show that they contain a central region consisting of 14 to 16 Gly-X-Y triplets. This region is flanked amino-terminal by a stretch of 14-23 proline residues and carboxy-terminal by a stretch of 6-9 prolines. At the NH2- and COOH-termini are repeated patterns of cysteine residues that are highly conserved between the molecules. A model is proposed which consists of a central stable collagen triple helix of 12-14 nm length from which three 9-22 nm long polyproline II type helices emerge at both ends. Disulfide linkage between cysteine-rich segments in these helices could lead to the formation of oligomeric network structures. Electrophoretic characterization of nematocyst extracts allows resolution of small proline-rich polypeptides that correspond in size to the cloned sequences.
我们已经分离并鉴定了四个与胶原蛋白相关的cDNA克隆(N-COL 1、N-COL 2、N-COL 3、N-COL 4),它们在水螅发育中的刺细胞中高度表达。所有这四个cDNA及其相应的转录本大小都很小(600-1000碱基对)。推导的氨基酸序列表明,它们含有一个由14至16个Gly-X-Y三联体组成的中心区域。该区域在氨基端侧翼为一段14-23个脯氨酸残基,在羧基端侧翼为一段6-9个脯氨酸。在NH2和COOH末端是分子间高度保守的半胱氨酸残基重复模式。提出了一个模型,该模型由一个长度为12-14纳米的中心稳定胶原三螺旋组成,两端伸出三个长度为9-22纳米的II型多聚脯氨酸螺旋。这些螺旋中富含半胱氨酸的片段之间的二硫键连接可能导致寡聚网络结构的形成。刺丝囊提取物的电泳特征能够分辨出大小与克隆序列相对应的富含脯氨酸的小多肽。