A thylakoid-localised FK506-binding protein in wheat may be linked to chloroplast biogenesis

Plant chloroplasts contain a large proportion of immunophilins, comprising the FK506-binding proteins (FKBPs) and cyclophilins (CYPs), which are members of the peptidyl-prolyl cis/trans isomerase (PPIase) family of proline-folding enzymes. Some of the chloroplastic immunophilins are known to chaperone certain photosynthetic proteins, however the functions of a majority of these proteins are unknown. This work focussed on characterisation of genes encoding the chloroplast-localised FKBP16-1 from wheat and its progenitor species, and identification of its putative promoters, as well as investigations into the effects of light regulation and plant development on its expression. The work identified several alternatively spliced FKBP16-1 transcripts, indicating expression of FKBP16-1 may be post-transcriptionally regulated. FKBP16-1 was expressed in both green and etiolated tissues, and highest levels were detected in developing tissues, indicating a role in chloroplast biogenesis. We also report a novel transcription module, designated 'chloroplast biogenesis module' (CBM) in the FKBP16-1 promoter of cereals that also appears to be involved in the regulation of additional genes involved in chloroplast biogenesis or other aspects of plant development. The results point to considerable potential for a role for FKBP16-1 in early chloroplast development, architecture of photosynthetic apparatus and plant development. (C) 2010 Elsevier Masson SAS. All rights reserved.