SOT1, a pentatricopeptide repeat protein with a small MutS-related domain, is required for correct processing of plastid 23S-4.5S rRNA precursors in Arabidopsis thaliana.

SOT1, a pentatricopeptide repeat protein with a small MutS-related domain, is required for correct processing of plastid 23S-4.5S rRNA precursors in Arabidopsis thaliana.
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SOT1 是一种具有小 MutS 相关结构域的五肽重复蛋白,是拟南芥中质体 23S-4.5S rRNA 前体的正确加工所必需的。

DOI:
10.1111/tpj.13126
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发表时间:
2016-03
期刊:
影响因子:
7.2
通讯作者:
Huang Jirong
Huang Jirong
中科院分区:
生物学1区
文献类型:
--
作者:
Wu Wenjuan;Liu Sheng;Ruwe Hannes;Zhang Delin;Melonek Joanna;Zhu Yajuan;Hu Xupeng;Gusewski S;ra;Yin Ping;Small Ian D;Howell Katharine A;Huang Jirong

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Ribosomal RNA processing is essential for plastid ribosome biogenesis, but is still poorly understood in higher plants. Here, we show that SUPPRESSOR OF THYLAKOID FORMATION1 (SOT1), a plastid-localized pentatricopeptide repeat (PPR) protein with a small MutS-related domain, is required for maturation of the 23S-4.5S rRNA dicistron. Loss of SOT1 function leads to slower chloroplast development, suppression of leaf variegation, and abnormal 23S and 4.5S processing. Predictions based on the PPR motif sequences identified the 5' end of the 23S-4.5S rRNA dicistronic precursor as a putative SOT1 binding site. This was confirmed by electrophoretic mobility shift assay, and by loss of the abundant small RNA 'footprint' associated with this site in sot1 mutants. We found that more than half of the 23S-4.5S rRNA dicistrons in sot1 mutants contain eroded and/or unprocessed 5' and 3' ends, and that the endonucleolytic cleavage product normally released from the 5' end of the precursor is absent in a sot1 null mutant. We postulate that SOT1 binding protects the 5' extremity of the 23S-4.5S rRNA dicistron from exonucleolytic attack, and favours formation of the RNA structure that allows endonucleolytic processing of its 5' and 3' ends.
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