Maize calreticulin localizes preferentially to plasmodesmata in root apex

Maize calreticulin localizes preferentially to plasmodesmata in root apex Summary Using a polyclonal antibody raised against calreticulin purified and sequenced from maize, we performed an immunocytological study to characterize putative domain‐specific subcellular distributions of endoplasmic reticulum (ER)‐resident calreticulin in meristematic cells of maize root tip. At the light microscopy level, calreticulin was immunolocalized preferentially at cellular peripheries, in addition to nuclear envelopes and cytoplasmic structures. Punctate labelling at the longitudinal walls and continuous labelling at the transverse walls was characteristic. Immunogold electron microscopy revealed plasmodesmata as the most prominently labelled cell periphery structure. In order to further probe the ER‐domain‐specific distribution of maize calreticulin at plasmodesmata, root apices were exposed to mannitol‐induced osmotic stress. Plasmolysis was associated with prominent accumulations of calreticulin at callose‐enriched plasmodesmata and pit fields while the contracting protoplasts were depleted of calreticulin. In contrast, other ER‐resident proteins recognized by HDEL peptide and BiP antibodies localized exclusively to contracted protoplasts. This finding reveals that, in plasmolysed cells, calreticulin enriched ER domains at plasmodesmata and pit fields are depleted of other ER‐resident proteins containing the HDEL retention peptide. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Plant Journal Wiley

Maize calreticulin localizes preferentially to plasmodesmata in root apex

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Publisher
Wiley
Copyright
Copyright © 1999 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0960-7412
eISSN
1365-313X
D.O.I.
10.1046/j.1365-313X.1999.00530.x
Publisher site
See Article on Publisher Site

Abstract

Summary Using a polyclonal antibody raised against calreticulin purified and sequenced from maize, we performed an immunocytological study to characterize putative domain‐specific subcellular distributions of endoplasmic reticulum (ER)‐resident calreticulin in meristematic cells of maize root tip. At the light microscopy level, calreticulin was immunolocalized preferentially at cellular peripheries, in addition to nuclear envelopes and cytoplasmic structures. Punctate labelling at the longitudinal walls and continuous labelling at the transverse walls was characteristic. Immunogold electron microscopy revealed plasmodesmata as the most prominently labelled cell periphery structure. In order to further probe the ER‐domain‐specific distribution of maize calreticulin at plasmodesmata, root apices were exposed to mannitol‐induced osmotic stress. Plasmolysis was associated with prominent accumulations of calreticulin at callose‐enriched plasmodesmata and pit fields while the contracting protoplasts were depleted of calreticulin. In contrast, other ER‐resident proteins recognized by HDEL peptide and BiP antibodies localized exclusively to contracted protoplasts. This finding reveals that, in plasmolysed cells, calreticulin enriched ER domains at plasmodesmata and pit fields are depleted of other ER‐resident proteins containing the HDEL retention peptide.

Journal

The Plant JournalWiley

Published: Aug 1, 1999

References

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