Journal
PLANT JOURNAL
Volume 103, Issue 4, Pages 1304-1317Publisher
WILEY
DOI: 10.1111/tpj.14802
Keywords
NaTrxh; Nicotiana alata; Self-incompatibility; S-RNase
Categories
Funding
- CONACyT-Mexico [434975]
- CONACyT [236602]
- PAPIIT-UNAM [IA204815, IN220919]
- US NSF [MCB 1127059]
- [FQ-5000-9128]
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In self-incompatible Solanaceae, the pistil protein S-RNase contributes toS-specific pollen rejection in conspecific crosses, as well as to rejecting pollen from foreign species or whole clades. However, S-RNase alone is not sufficient for either type of pollen rejection. We describe a thioredoxin (Trx) type h fromNicotiana alata, NaTrxh, which interacts with and reduces S-RNasein vitro. Here, we show that expressing a redox-inactive mutant, NaTrxh(SS), suppresses bothS-specific pollen rejection and rejection of pollen fromNicotiana plumbaginifolia. Biochemical experiments provide evidence that NaTrxh specifically reduces the Cys(155)-Cys(185)disulphide bond ofS(C10)-Rnase, resulting in a significant increase of its ribonuclease activity. This reduction and increase in S-RNase activity by NaTrxh helps to explain why S-RNase alone could be insufficient for pollen rejection.
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