Summary
The cytosolic chaperonin containing t-complex peptide-1 (CCT) is involved in the correct folding of newly synthetized actin and tubulin molecules. To get insight into potential additional functions of plant CCT, the localization of the subunit CCTɛ was followed throughout cell cycle, cell elongation, and cell differentiation in the tobacco cell culture VBI-O with relation to the microtubular cytoskeleton by double-immunofluorescence and confocal microscopy. The CCTɛ subunit was found to colocalize with sites of microtubule nucleation such as nuclear envelope and preprophase band. In addition, CCTɛ was associated with tubulin in sites of elevated wall synthesis such as phragmoplast or along secondary-wall thickenings. CCTɛ and its substrate tubulin were found to be soluble during periods of cytoskeletal dynamics, whereas sedimentable, vesicle-bound forms of CCTɛ and tubulin prevailed during cell differentiation. The sedimentability of CCTɛ was increased by calcium, whereas it was detached from microsomes by ATP. CCTɛ can bind to both polymerized microtubules and tubulin dimers. These data suggest an additional function of plant CCT in microtubule-driven transport of vesicles that contain cell-wall material.
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Abbreviations
- CCT:
-
cytosolic chaperonin containing t-complex polypeptide 1
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Nick, P., Heuing, A. & Ehmann, B. Plant chaperonins: a role in microtubule-dependent wall formation?. Protoplasma 211, 234–244 (2000). https://doi.org/10.1007/BF01304491
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DOI: https://doi.org/10.1007/BF01304491