Apple S-RNase triggers inhibition of tRNA aminoacylation by interacting with a soluble inorganic pyrophosphatase in growing self-pollen tubes in vitro

© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 218(2018), 2 vom: 01. Apr., Seite 579-593
1. Verfasser: Li, Wei (VerfasserIn)
Weitere Verfasser: Meng, Dong, Gu, Zhaoyu, Yang, Qing, Yuan, Hui, Li, Yang, Chen, Qiuju, Yu, Jie, Liu, Chunsheng, Li, Tianzhong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Malus domestica MdPPa PPi accumulation S-RNase aminoacylation of tRNA pollen tube growth Diphosphates Ribonucleases mehr... EC 3.1.- Inorganic Pyrophosphatase EC 3.6.1.1
Beschreibung
Zusammenfassung:© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.
Apple exhibits S-RNase-based self-incompatibility (SI), in which S-RNase plays a central role in rejecting self-pollen. It has been proposed that the arrest of pollen growth in SI of Solanaceae plants is a consequence of the degradation of pollen rRNA by S-RNase; however, the underlying mechanism in Rosaceae is still unclear. Here, we used S2 -RNase as a bait to screen an apple pollen cDNA library and characterized an apple soluble inorganic pyrophosphatase (MdPPa) that physically interacted with S-RNases. When treated with self S-RNases, apple pollen tubes showed a marked growth inhibition, as well as a decrease in endogenous soluble pyrophosphatase activity and elevated levels of inorganic pyrophosphate (PPi). In addition, S-RNase was found to bind to two variable regions of MdPPa, resulting in a noncompetitive inhibition of its activity. Silencing of MdPPa expression led to a reduction in pollen tube growth. Interestingly, tRNA aminoacylation was inhibited in self S-RNase-treated or MdPPa-silenced pollen tubes, resulting in the accumulation of uncharged tRNA. Furthermore, we provide evidence showing that this disturbance of tRNA aminoacylation is independent of RNase activity. We propose an alternative mechanism differing from RNA degradation to explain the cytotoxicity of the S-RNase apple SI process
Beschreibung:Date Completed 19.09.2019
Date Revised 30.09.2020
published: Print-Electronic
GENBANK: XM_008360526, D50837, U12199, U12200, U19793
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.15028