期刊
NUCLEIC ACIDS RESEARCH
卷 43, 期 3, 页码 1918-1926出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv027
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资金
- Australian Research Council (Discovery Project) [DP120102870]
- Pearl Technologies Ltd
- University of Western Australia
- The University of Western Australia
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1243641] Funding Source: National Science Foundation
The pentatricopeptide repeat (PPR) protein family is a large family of RNA-binding proteins that is characterized by tandem arrays of a degenerate 35-amino-acid motif which form an alpha-solenoid structure. PPR proteins influence the editing, splicing, translation and stability of specific RNAs in mitochondria and chloroplasts. Zea mays PPR10 is amongst the best studied PPR proteins, where sequence-specific binding to two RNA transcripts, atpH and psaJ, has been demonstrated to follow a recognition code where the identity of two amino acids per repeat determines the base-specificity. A recently solved ZmPPR10:psaJ complex crystal structure suggested a homodimeric complex with considerably fewer sequence-specific protein-RNA contacts than inferred previously. Here we describe the solution structure of the ZmPPR10: atpH complex using size-exclusion chromatography-coupled synchrotron small-angle X-ray scattering (SEC-SYSAXS). Our results support prior evidence that PPR10 binds RNA as a monomer, and that it does so in a manner that is commensurate with a canonical and predictable RNA-binding mode across much of the RNA-protein interface.
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