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J Biol Chem. 2014 Nov 7;289(45):31503-12. doi: 10.1074/jbc.M114.575472. Epub 2014 Sep 17.

Examination of the dimerization states of the single-stranded RNA recognition protein pentatricopeptide repeat 10 (PPR10).

Author information

1
From the State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and.
2
Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and Ministry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
3
the State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China, and.
4
the National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, and College of Life Sciences and Technology, Huazhong Agricultural University, Wuhan 430070, China yinping@mail.hzau.edu.cn.
5
From the State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua-Peking Center for Life Sciences, and nyan@tsinghua.edu.cn.

Abstract

Pentatricopeptide repeat (PPR) proteins, particularly abundant in plastids and mitochrondria of angiosperms, include a large number of sequence-specific RNA binding proteins that are involved in diverse aspects of organelle RNA metabolisms. PPR proteins contain multiple tandom repeats, and each repeat can specifically recognize a RNA base through residues 2, 5, and 35 in a modular fashion. The crystal structure of PPR10 from maize chloroplast exhibits dimeric existence both in the absence and presence of the 18-nucleotide psaJ RNA element. However, previous biochemical analysis suggested a monomeric shift of PPR10 upon RNA binding. In this report, we show that the amino-terminal segments of PPR10 determine the dimerization state of PPR10. A single amino acid alteration of cysteine to serine within repeat 10 of PPR10 further drives dimerization of PPR10. The biochemical elucidation of the determinants for PPR10 dimerization may provide an important foundation to understand the working mechanisms of PPR proteins underlying their diverse physiological functions.

KEYWORDS:

Cell Biology; Crystal Structure; Protein-Nucleic Acid Interaction; RNA; RNA Binding Protein; RNA-Protein Interaction

PMID:
25231995
PMCID:
PMC4223348
DOI:
10.1074/jbc.M114.575472
[Indexed for MEDLINE]
Free PMC Article

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