Functional characterization of chaperonin containing T-complex polypeptide-1 and its conserved and novel substrates in Arabidopsis

© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 70(2019), 10 vom: 09. Mai, Seite 2741-2757
1. Verfasser: Ahn, Hee-Kyung (VerfasserIn)
Weitere Verfasser: Yoon, Joong-Tak, Choi, Ilyeong, Kim, Sumin, Lee, Ho-Seok, Pai, Hyun-Sook
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't CCT chaperonin PP4 catalytic subunit TOR signaling pathway Tap46 tubulin biogenesis virus-induced gene silencing Arabidopsis Proteins CENTRAL CITY protein, Arabidopsis mehr... Repressor Proteins Tubulin
Beschreibung
Zusammenfassung:© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.
Chaperonin containing T-complex polypeptide-1 (CCT) is an evolutionarily conserved chaperonin multi-subunit complex that mediates protein folding in eukaryotes. It is essential for cell growth and survival in yeast and mammals, with diverse substrate proteins. However, only a few studies on plant CCT have been reported to date, due to the essentiality of CCT subunit genes and the large size of the complex. Here, we have investigated the structure and function of the Arabidopsis CCT complex in detail. The plant CCT consisted of eight subunits that assemble to form a high-molecular-mass protein complex, shown by diverse methods. CCT-deficient cells exhibited depletion of cortical microtubules, accompanied by a reduction in cellular α- and β-tubulin levels due to protein degradation. Cycloheximide-chase assays suggested that CCT is involved in the folding of tubulins in plants. Furthermore, CCT interacted with PPX1, the catalytic subunit of protein phosphatase 4, and may participate in the folding of PPX1 as its substrate. CCT also interacted with Tap46, a regulatory subunit of PP2A family phosphatases, but Tap46 appeared to function in PPX1 stabilization, rather than as a CCT substrate. Collectively, our findings reveal the essential functions of CCT chaperonin in plants and its conserved and novel substrates
Beschreibung:Date Completed 06.07.2020
Date Revised 06.07.2020
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erz099