The acidic domain of the chloroplast RNA-binding protein CP31A supports cold tolerance in Arabidopsis thaliana. (19th April 2021)

• Record Type: Journal Article
• Authors: Okuzaki, Ayako; Rühle, Thilo; Leister, Dario; Schmitz-Linneweber, Christian
• Editors: Sharwood, Robert
• Is Part Of: Journal of experimental botany. Volume 72:Number 13(2021)
• Page Start: 4904
• Page End: 4914
• Publication Date: 2021-04-19
• Subjects: Acidic domain -- Arabidopsis thaliana -- chloroplast -- NDH complex -- organelle -- RNA editing -- RNA processing -- RNA stability; Botany -- Periodicals; Botany, Experimental -- Periodicals; Plant physiology -- Periodicals; 580
• DOI: 10.1093/jxb/erab165
• Languages: English
• ISSNs: 0022-0957

Abstract

Abstract : Arabidopsis chloroplast development under cold conditions critically depends on the acidic domain of the RNA-binding protein CP31A. Abstract: The processing of chloroplast RNA requires a large number of nuclear-encoded RNA-binding proteins (RBPs) that are imported post-translationally into the organelle. The chloroplast ribonucleoprotein 31A (CP31A) supports RNA editing at 13 sites and also supports the accumulation of multiple chloroplast mRNAs. In cp31a mutants it is the ndhF mRNA (coding for a subunit of the NDH complex) that is most strongly affected. CP31A becomes particularly important at low temperatures, where it is essential for chloroplast development in young tissue. Next to two RNA-recognition motifs (RRMs), CP31A has an N-terminal acidic domain that is phosphorylated at several sites. We investigated the function of the acidic domain in the role of CP31A in RNA metabolism and cold resistance. Using point mutagenesis, we demonstrate that the known phosphorylation sites within the acidic domain are irrelevant for any of the known functions of CP31A, both at normal and at low temperatures. Even when the entire acidic domain is removed, no effects on RNA editing were observed. By contrast, loss of the acidic domain reduced the ability of CP31A to stabilize the ndhF mRNA, which was associated with reduced NDH complex activity. Most importantly, acidic domain-less CP31A lines displayed bleached young tissue in the cold. Together, these data show that the different functions of CP31A can be assigned to different regions of the protein: the RRMs are sufficient to maintain RNA editing and to allow the accumulation of basal amounts of ndhF mRNA, while chloroplast development under cold conditions critically depends on the acidic domain.