Physcomitrium patens pentatricopeptide repeat protein PpPPR_32 is involved in the accumulation of psaC mRNA encoding the iron sulfur protein of photosystem I. (9th March 2022)

• Record Type: Journal Article
• Authors: Suzuki, Ryo; Sugita, Chieko; Aoki, Setsuyuki; Sugita, Mamoru
• Is Part Of: Genes to cells. Volume 27:Number 4(2022)
• Page Start: 293
• Page End: 304
• Publication Date: 2022-03-09
• Subjects: basal land plant -- chloroplast -- photosystem I -- Physcomitrium patens -- plastid -- PPR protein I psaC -- RNA accumulation; Cytogenetics -- Periodicals; Cells -- Mechanical properties -- Periodicals; Molecular genetics -- Periodicals; Genes -- Periodicals; Molecular biology -- Periodicals; Cytology -- Periodicals; Biomechanics -- Periodicals; 571.6
• DOI: 10.1111/gtc.12928
• Languages: English
• ISSNs: 1356-9597

Abstract

Abstract: Pentatricopeptide repeat (PPR) proteins are involved in RNA metabolism and also play a role in posttranscriptional regulation during plant organellar gene expression. Although a hundred of PPR proteins exist in the moss Physcomitrium patens, their functions are not fully understood. Here, we report the function of P‐class PPR protein PpPPR_32 in P. patens . A transient expression assay using green fluorescent protein demonstrated that the N‐terminal region of PpPPR_32 functions as a chloroplast‐targeting transit peptide, indicating that PpPPR_32 is localized in chloroplasts. PpPPR_32 knockout mutants grew autotrophically but with reduced protonema growth and the poor formation of photosystem I (PSI) complexes. Quantitative real‐time reverse transcription‐polymerase chain reaction and RNA gel blot hybridization analyses revealed a significant reduction in the transcript level of the psaC gene encoding the iron sulfur protein of PSI but no alteration to the transcript levels of other PSI genes. This suggests that PpPPR_32 is specifically involved in the expression level of the psaC gene. Our results indicate that PpPPR_32 is essential for the accumulation of psaC transcript and PSI complexes.