IDENTIFICATION OF A HIGHLY CONSERVED HYDROXYPROLINE-RICH GLYCOPROTEIN IN THE CELL-WALLS OF CHLAMYDOMONAS-REINHARDTII AND 2 OTHER VOLVOCALES
IDENTIFICATION OF A HIGHLY CONSERVED HYDROXYPROLINE-RICH GLYCOPROTEIN IN THE CELL-WALLS OF CHLAMYDOMONAS-REINHARDTII AND 2 OTHER VOLVOCALES
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DOI：
10.1007/bf00391084
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发表时间：
1989-10-01
期刊：
影响因子：
4.3
通讯作者：
APPEL, H
中科院分区：
文献类型：
--
作者：
ADAIR, WS;APPEL, H
单细胞藻类莱茵衣藻（Chlamydomonas reinhardtii Dang）的细胞壁完全由富含羟基脯氨酸的糖蛋白（HRGPs）构成。最近，我们采用了一种体外定量重组系统（Adair et al. 1987， J. Cell Biol. 105, 2373-2382），将C. reinhardtii的外壁HRGPs分配到特定的亚层，并描述了负责其组装的主要相互作用。其中一些相互作用似乎涉及相对保守的HRGP结构域，如reinhardtii和两种多细胞涡旋（Volvox carteri lyengar和Gonium pectorale Muller）之间的种间细胞壁重构。在本报告中，我们提供了生化和免疫学证据，证明V. carteri和G. pectorale的外细胞壁都含有与C. reinhardtii GP2密切相关的突出hrgp。保守的GP2同源物的鉴定表明了种间重构的分子基础，并为表征介导这些藻类细胞壁形成的HRGP结构域提供了有用的途径。
The unicellular alga (Chlamydomonas reinhardtii Dang, has a cell wall made entirely from hydroxyproline-rich glycoproteins (HRGPs). We recently employed a quantitative in vitro reconstitution system (Adair et al. 1987, J. Cell Biol. 105, 2373-2382) to assign outer-wall HRGPs of C. reinhardtii to specific sublayers, and describe the major interactions responsible for their assembly. Some of these interactions appear to involve relatively conserved HRGP domains, as evidenced by interspecific cell-wall reconstitution between C. reinhardtii and two multicellular Volvocales (Volvox carteri lyengar and Gonium pectorale Muller). In the present report we provide biochemical and immunological evidence that the outer cell-walls of V. carteri and G. pectorale both contain prominent HRGPs closely related to C. reinhardtii GP2. Identification of conserved GP2 homologues indicates a molecular basis for interspecific reconstitution and provides a useful avenue for characterization of HRGP domains mediating cell-wall formation in these algae.