A chloroplast-targeted DnaJ protein AtJ8 is negatively regulated by light and has rapid turnover in darkness.

The DnaJ proteins (also called as J proteins, J domain proteins or HSP40 proteins) function as molecular co-chaperones for the HSP70 proteins. We assessed the expression of the small chloroplast-targeted DnaJ protein, the AtJ8 protein, by subjecting the wild type Arabidopsis plants to different illumination conditions. It is shown that the expression of the transcripts and proteins of the ATJ8 gene is primarily regulated at the level of transcription. When plants were incubated under high light for 3h, both the transcripts and proteins were completely abolished. Upon transfer of plants to darkness, the transcripts started rapidly accumulating, and subsequently, the AtJ8 protein became visible after 2h in darkness. Conversely, incubation of plants in darkness or under low light intensities induced expression of the ATJ8 transcripts and proteins. Feeding plants with sugars clearly decreased the transcript and protein levels, and incubation with cycloheximide revealed a rapid turnover for AtJ8 in darkness. Moreover, the AtJ8 protein was found to be nearly missing from the var1 mutant, which lacks the FTSH5 protease. It is concluded that AtJ8 is expressed mainly in darkness, is prone to a rapid turnover but is partially stabilized by the FTSH proteases.