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Localization of pyrophosphatase and V-ATPase in Chlamydomonas reinhardtii

Robinson, D. G. and Hoppenrath, Mona and Oberbeck, K. and Luykx, P. and Ratajczak, R. (1998):
Localization of pyrophosphatase and V-ATPase in Chlamydomonas reinhardtii.
In: Plant biology, 111 (2), Wiley, pp. 108-122, ISSN 1435-8603,
[Online-Edition: https://doi.org/10.1111/j.1438-8677.1998.tb00685.x],
[Article]

Abstract

Microsomal membranes of Chlamydomonas reinhardtii possess PPase and V‐ATPase activities. By immunogold labelling we have shown that H+‐pyrophosphatase (PPase) is localized to membranes of lytic and contractile vacuoles of Chlamydomonas, in which the density of antigen in the latter is much higher. In addition, PPase is conspicuously present in trans cisternae and transpole elements of the Colgi apparatus. Such a distribution for PPase has hitherto not been reported. A positive in situ identification for PPase at the plasma membrane, including the flagellar membrane, was also made, and has also been confirmed by Western blotting and activity measurements on isolated plasma membranes. V‐ATPase antisera which cross react with polypeptides of this transport complex from maize roots failed to recognize anything in Western blots of Chlamydomonas microsomal membranes. Thus immunogold labelling for V‐ATPase was not possible with Chlamydomonas. On the other hand, surfaces of contractile vacuole membranes as revealed by deepetching were covered by conspicuous 9 − 11.5 nm diameter smooth particles which had a central hole. These were very similar to those previously identified by Heuser et al., (1993) as the V,‐head of V‐ATPase in Dictyostelium contractile vacuoles. Another type of membrane image, designated “intermediate‐sized vesicle”, was found associated with the contractile vacuole. It was characterized by densely‐packed 6 − 7.5nm diameter polygonal particles, which upon rotation analysis showed both 5‐ and 6‐fold symmetries, also with a central hole. These particles are interpreted as representing either PPase complexes or the V0 body of the V‐ATPase in etched fractured membrane surfaces. We have incorporated these findings into a model of contractile vacuole function.

Item Type: Article
Erschienen: 1998
Creators: Robinson, D. G. and Hoppenrath, Mona and Oberbeck, K. and Luykx, P. and Ratajczak, R.
Title: Localization of pyrophosphatase and V-ATPase in Chlamydomonas reinhardtii
Language: English
Abstract:

Microsomal membranes of Chlamydomonas reinhardtii possess PPase and V‐ATPase activities. By immunogold labelling we have shown that H+‐pyrophosphatase (PPase) is localized to membranes of lytic and contractile vacuoles of Chlamydomonas, in which the density of antigen in the latter is much higher. In addition, PPase is conspicuously present in trans cisternae and transpole elements of the Colgi apparatus. Such a distribution for PPase has hitherto not been reported. A positive in situ identification for PPase at the plasma membrane, including the flagellar membrane, was also made, and has also been confirmed by Western blotting and activity measurements on isolated plasma membranes. V‐ATPase antisera which cross react with polypeptides of this transport complex from maize roots failed to recognize anything in Western blots of Chlamydomonas microsomal membranes. Thus immunogold labelling for V‐ATPase was not possible with Chlamydomonas. On the other hand, surfaces of contractile vacuole membranes as revealed by deepetching were covered by conspicuous 9 − 11.5 nm diameter smooth particles which had a central hole. These were very similar to those previously identified by Heuser et al., (1993) as the V,‐head of V‐ATPase in Dictyostelium contractile vacuoles. Another type of membrane image, designated “intermediate‐sized vesicle”, was found associated with the contractile vacuole. It was characterized by densely‐packed 6 − 7.5nm diameter polygonal particles, which upon rotation analysis showed both 5‐ and 6‐fold symmetries, also with a central hole. These particles are interpreted as representing either PPase complexes or the V0 body of the V‐ATPase in etched fractured membrane surfaces. We have incorporated these findings into a model of contractile vacuole function.

Journal or Publication Title: Plant biology
Volume: 111
Number: 2
Publisher: Wiley
Divisions: 10 Department of Biology
Date Deposited: 19 Nov 2008 16:19
Official URL: https://doi.org/10.1111/j.1438-8677.1998.tb00685.x
License: [undefiniert]
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