UBC19 is a new interacting protein of ORANGE for its nuclear localization in Arabidopsis thaliana. (2nd November 2021)

• Record Type: Journal Article
• Authors: Chen, Wei-Cai; Wang, Qi; Cao, Tian-Jun; Lu, Shan
• Is Part Of: Plant signaling & behavior. Volume 16:Number 11(2021)
• Publication Date: 2021-11-02
• Subjects: De-etiolation -- nucleus -- ORANGE -- protein-protein interaction -- UBC19; Plant ecophysiology -- Periodicals; Plant cellular signal transduction -- Periodicals; Plant cellular signal transduction; Plant ecophysiology; Periodicals; Electronic journals; 581
• DOI: 10.1080/15592324.2021.1964847
• Languages: English
• ISSNs: 1559-2316

Abstract

ABSTRACT: ORANGE (OR) is a member of the DnaJ-like zinc finger domain-containing protein family, of which all orthologs share a highly conserved quadruple repeat of the CxxCxxxG signatures at their C-termini. Dual subcellular localization and different interacting partner proteins have been reported for OR. In plastids, OR interacts with phytoene synthase, the entry enzyme for carotenoid biosynthesis, to promote chromoplast biogenesis and carotenoid accumulation in non-pigmented tissues. In the nucleus, OR interacts with the eukaryotic release factor eRF1-2 to regulate cell elongation in the petiole, and with the transcription factor TCP14 to repress the expression of Early Light-Induced Proteins ( ELIPs ) and chloroplast biogenesis in de-etiolating cotyledons. In this study, we demonstrated the E2 ubiquitin-conjugating enzyme UBC19 as a new interacting partner of OR. The lysine 58 of OR was found to be ubiquitinated, and OR lost its nuclear localization and the capability in repressing ELIPs when lysine 58 was substituted by alanine. Our findings raised the possibility that the ubiquitination by UBC19 is essential for the nuclear localization of OR.