A temporal gradient of cytonuclear coordination of chaperonins and chaperones during RuBisCo biogenesis in allopolyploid plants

Proc Natl Acad Sci U S A. 2022 Aug 23;119(34):e2200106119. doi: 10.1073/pnas.2200106119. Epub 2022 Aug 15.

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCo) has long been studied from many perspectives. As a multisubunit (large subunits [LSUs] and small subunits[SSUs]) protein encoded by genes residing in the chloroplast (rbcL) and nuclear (rbcS) genomes, RuBisCo also is a model for cytonuclear coevolution following allopolyploid speciation in plants. Here, we studied the genomic and transcriptional cytonuclear coordination of auxiliary chaperonin and chaperones that facilitate RuBisCo biogenesis across multiple natural and artificially synthesized plant allopolyploids. We found similar genomic and transcriptional cytonuclear responses, including respective paternal-to-maternal conversions and maternal homeologous biased expression, in chaperonin/chaperon-assisted folding and assembly of RuBisCo in different allopolyploids. One observation is about the temporally attenuated genomic and transcriptional cytonuclear evolutionary responses during early folding and later assembly process of RuBisCo biogenesis, which were established by long-term evolution and immediate onset of allopolyploidy, respectively. Our study not only points to the potential widespread and hitherto unrecognized features of cytonuclear evolution but also bears implications for the structural interaction interface between LSU and Cpn60 chaperonin and the functioning stage of the Raf2 chaperone.

Keywords: RuBisCo; allopolyploids; chaperone; chaperonin; cytonuclear coevolution/coordination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Nucleus / metabolism
  • Chaperonin 60 / genetics
  • Chaperonin 60 / metabolism
  • Chaperonins / metabolism*
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Plant Proteins / metabolism*
  • Plants / metabolism
  • Ribulose-Bisphosphate Carboxylase* / metabolism

Substances

  • Chaperonin 60
  • Molecular Chaperones
  • Plant Proteins
  • Chaperonins
  • Ribulose-Bisphosphate Carboxylase