NaTrxh is an essential protein for pollen rejection in Nicotiana by increasing S-RNase activity

Plant J. 2020 Aug;103(4):1304-1317. doi: 10.1111/tpj.14802. Epub 2020 Jun 13.

Abstract

In self-incompatible Solanaceae, the pistil protein S-RNase contributes to S-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 from Nicotiana alata, NaTrxh, which interacts with and reduces S-RNase in vitro. Here, we show that expressing a redox-inactive mutant, NaTrxhSS , suppresses both S-specific pollen rejection and rejection of pollen from Nicotiana plumbaginifolia. Biochemical experiments provide evidence that NaTrxh specifically reduces the Cys155 -Cys185 disulphide bond of SC10 -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.

Keywords: NaTrxh; Nicotiana alata; S-RNase; Self-incompatibility.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Flowers / genetics
  • Flowers / metabolism
  • Flowers / physiology
  • Nicotiana / genetics
  • Nicotiana / metabolism*
  • Nicotiana / physiology*
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Pollen / genetics
  • Pollen / metabolism*
  • Pollen / physiology*
  • Ribonucleases / genetics
  • Ribonucleases / metabolism*

Substances

  • Plant Proteins
  • Ribonucleases
  • ribonuclease S