Structure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA Recognition

doi:10.1074/jbc.M113.496828

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	Structure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA Recognition
	Ban, Ting 2,3,4; Ke, Jiyuan 5; Chen, Runze 4; Gu, Xin 5; Tan, M. H. Eileen 5,6; Zhou, X. Edward 5; Kang, Yanyong 5; Melcher, Karsten 5; Zhu, Jian-Kang 1,2,3; Xu, H. Eric4,5
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2013-11-01
卷号	288 期号:44 页码:31540-31548
ISSN号	0021-9258
DOI	10.1074/jbc.M113.496828
文献子类	Article
英文摘要	Pentatricopeptide repeat (PPR) proteins are sequence-specific RNA-binding proteins that form a pervasive family of proteins conserved in yeast, plants, and humans. The plant PPR proteins are grouped mainly into the P and PLS classes. Here, we report the crystal structure of a PLS-class PPR protein from Arabidopsis thaliana called THA8L (THA8-like) at 2.0 angstrom. THA8L resembles THA8 (thylakoid assembly 8), a protein that is required for the splicing of specific group II introns of genes involved in biogenesis of chloroplast thylakoid membranes. The THA8L structure contains three P-type PPR motifs flanked by one L-type motif and one S-type motif. We identified several putative THA8L-binding sites, enriched with purine sequences, in the group II introns. Importantly, THA8L has strong binding preference for single-stranded RNA over single-stranded DNA or double-stranded RNA. Structural analysis revealed that THA8L contains two extensive patches of positively charged residues next to the residues that are proposed to comprise the RNA-binding codes. Mutations in these two positively charged patches greatly reduced THA8L RNA-binding activity. On the basis of these data, we constructed a model of THA8L-RNA binding that is dependent on two forces: one is the interaction between nucleotide bases and specific amino acids in the PPR motifs (codes), and the other is the interaction between the negatively charged RNA backbone and positively charged residues of PPR motifs. Together, these results further our understanding of the mechanism of PPR protein-RNA interactions.
资助项目	NIDDK NIH HHS[R01 DK071662]
WOS关键词	MESSENGER-RNA ; PPR PROTEINS ; CHLOROPLASTS ; ARABIDOPSIS ; IDENTIFICATION ; STABILIZATION ; CHLAMYDOMONAS ; BINDING ; TERMINI
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
WOS记录号	WOS:000330596200013
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/277387]
专题	药物靶标结构与功能中心
通讯作者	Zhu, Jian-Kang
作者单位	1.Purdue Univ, Dept Hort & Landscape Architecture, W Lafayette, IN 47906 USA 2.Chinese Acad Sci, Shanghai Ctr Plant Stress Biol, Shanghai 200032, Peoples R China; 3.Chinese Acad Sci, Shanghai Inst Plant Physiol & Ecol, Shanghai Inst Biol Sci, Shanghai 200032, Peoples R China; 4.Chinese Acad Sci, Shanghai Inst Mat Med, Van Andel Res Inst Shanghai Inst Mat Med ARI SIMM, Ctr Struct & Funct Drug Targets,Key Lab Receptor, Shanghai 201203, Peoples R China; 5.Ctr Struct Biol & Drug Discovery, Van Andel Res Inst, Lab Struct Sci, Grand Rapids, MI 49503 USA; 6.Natl Univ Singapore, Yong Loo Lin Sch Med, Natl Univ Hosp, Dept Obstet & Gynecol, Singapore 119228, Singapore;
推荐引用方式 GB/T 7714	Ban, Ting,Ke, Jiyuan,Chen, Runze,et al. Structure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA Recognition[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2013,288(44):31540-31548.
APA	Ban, Ting.,Ke, Jiyuan.,Chen, Runze.,Gu, Xin.,Tan, M. H. Eileen.,...&Xu, H. Eric.(2013).Structure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA Recognition.JOURNAL OF BIOLOGICAL CHEMISTRY,288(44),31540-31548.
MLA	Ban, Ting,et al."Structure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA Recognition".JOURNAL OF BIOLOGICAL CHEMISTRY 288.44(2013):31540-31548.