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5GI0

Crystal structure of RNA editing factor MORF9/RIP9

Summary for 5GI0
Entry DOI10.2210/pdb5gi0/pdb
DescriptorMultiple organellar RNA editing factor 9, chloroplastic (2 entities in total)
Functional Keywordsrna editing factor, morf9, rip9, rna binding protein
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Cellular locationPlastid, chloroplast : Q9LPZ1
Total number of polymer chains1
Total formula weight15734.68
Authors
Yan, J.,Zhang, Q.,Guan, Z.,Zou, T.,Yin, P. (deposition date: 2016-06-21, release date: 2017-05-10, Last modification date: 2024-10-16)
Primary citationYan, J.,Zhang, Q.,Guan, Z.,Wang, Q.,Li, L.,Ruan, F.,Lin, R.,Zou, T.,Yin, P.
MORF9 increases the RNA-binding activity of PLS-type pentatricopeptide repeat protein in plastid RNA editing
Nat Plants, 3:17037-17037, 2017
Cited by
PubMed Abstract: RNA editing is a post-transcriptional process that modifies the genetic information on RNA molecules. In flowering plants, RNA editing usually alters cytidine to uridine in plastids and mitochondria. The PLS-type pentatricopeptide repeat (PPR) protein and the multiple organellar RNA editing factor (MORF, also known as RNA editing factor interacting protein (RIP)) are two types of key trans-acting factors involved in this process. However, how they cooperate with one another remains unclear. Here, we have characterized the interactions between a designer PLS-type PPR protein (PLS)PPR and MORF9, and found that RNA-binding activity of (PLS)PPR is drastically increased on MORF9 binding. We also determined the crystal structures of (PLS)PPR, MORF9 and the (PLS)PPR-MORF9 complex. MORF9 binding induces significant compressed conformational changes of (PLS)PPR, revealing the molecular mechanisms by which MORF9-bound (PLS)PPR has increased RNA-binding activity. Similarly, increased RNA-binding activity is observed for the natural PLS-type PPR protein, LPA66, in the presence of MORF9. These findings significantly expand our understanding of MORF function in plant organellar RNA editing.
PubMed: 28394309
DOI: 10.1038/nplants.2017.37
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.044 Å)
Structure validation

226707

건을2024-10-30부터공개중

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