Identification of a highly conserved hydroxyproline-rich glycoprotein in the cell walls of Chlamydomonas reinhardtii and two other Volvocales |
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Authors: | W Steven Adair Heidi Appel |
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Institution: | (1) Biology Department, Washington University, 63130 St. Louis, MO, USA;(2) Present address: Department of Anatomy and Cellular Biology, Tufts School of Medicine, 136 Harrison Avenue, 02111 Boston, MA, USA |
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Abstract: | The unicellular alga Chlamydomonas reinhardtii Dang, has a cell wall made entirely from hydroxyproline-rich glycoproteins (HRGPs). We recently employed a quantiative 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 (Volvoxcarteri lyengar and Gonium pectorale Müller). 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.Abbreviations GP1, 2, 3
outer-cell wall glycoproteins 1, 2, and 3
- GP2dg
deglycosylated GP2
- HRGP
hydroxyprolinerich glycoprotein
- SDS-PAGE
sodium docecyl sulfate polyacrylamide gel electrophoresis |
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Keywords: | Chlamydomonas Cell wall (Volvocales) Hydroxyproline-rich cell wall glycoproteins Volvocales (evolution) |
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