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Tracking the elusive 5′ exonuclease activity of Chlamydomonas reinhardtii RNase J

Liponska, A. and Jamalli, A. and Kuras, R. and Suay, L. and Garbe, E. and Wollman, F.-A. and Laalami, S. and Putzer, H. (2018) Tracking the elusive 5′ exonuclease activity of Chlamydomonas reinhardtii RNase J. Plant Molecular Biology. pp. 1-13.

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Key message: Chlamydomonas RNase J is the first member of this enzyme family that has endo- but no intrinsic 5′ exoribonucleolytic activity. This questions its proposed role in chloroplast mRNA maturation. Abstract: RNA maturation and stability in the chloroplast are controlled by nuclear-encoded ribonucleases and RNA binding proteins. Notably, mRNA 5′ end maturation is thought to be achieved by the combined action of a 5′ exoribonuclease and specific pentatricopeptide repeat proteins (PPR) that block the progression of the nuclease. In Arabidopsis the 5′ exo- and endoribonuclease RNase J has been implicated in this process. Here, we verified the chloroplast localization of the orthologous Chlamydomonas (Cr) RNase J and studied its activity, both in vitro and in vivo in a heterologous B. subtilis system. Our data show that Cr RNase J has endo- but no significant intrinsic 5′ exonuclease activity that would be compatible with its proposed role in mRNA maturation. This is the first example of an RNase J ortholog that does not possess a 5′ exonuclease activity. A yeast two-hybrid screen revealed a number of potential interaction partners but three of the most promising candidates tested, failed to induce the latent exonuclease activity of Cr RNase J. We still favor the hypothesis that Cr RNase J plays an important role in RNA metabolism, but our findings suggest that it rather acts as an endoribonuclease in the chloroplast. © 2018 Springer Science+Business Media B.V., part of Springer Nature

Item Type: Article
Additional Information: cited By 0; Article in Press
Subjects: مقالات نمایه شده محققین دانشگاه در سایت ,Web of Science ,Scopus
Depositing User: GOUMS
Date Deposited: 16 Apr 2018 05:02
Last Modified: 16 Apr 2018 05:02
URI: http://eprints.goums.ac.ir/id/eprint/9532

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