Recent progress toward RNA manipulation with engineered pentatricopeptide repeat proteins

Takayoshi Imai, Yusuke Yagi, Takahiro Nakamura

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Pentatricopeptide repeat (PPR) proteins are RNA-binding proteins that are widely distributed in plants. They contain 2 to 30 repeating units of ~35-amino acid PPR motifs. They are known to play important roles in RNA processing, RNA editing, and translational regulation. Recent studies on the RNA recognition mode of PPR proteins revealed that one PPR motif interacts with one nucleotide. In addition, it was revealed that amino acids at three specific positions in a single motif serve to specify its binding base. Thus, mutation of these amino acids can cause a modification of the binding specificity of PPR motifs. Indeed, the engineered PPR motifs fused with various effector domains are shown to bind to and manipulate RNAs in a controlled manner. In this review, we summarize the recent progress in structural studies on PPR motifs. We focus on their RNA recognition mode and discuss the potentials of PPR as novel, versatile tools for RNA manipulation.

Original languageEnglish
Title of host publicationApplied RNA Bioscience
PublisherSpringer Singapore
Pages151-160
Number of pages10
ISBN (Electronic)9789811083723
ISBN (Print)9789811083716
DOIs
Publication statusPublished - Apr 10 2018

Fingerprint

RNA
Proteins
Amino Acids
RNA Editing
RNA-Binding Proteins
Nucleotides
Mutation
Processing

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Recent progress toward RNA manipulation with engineered pentatricopeptide repeat proteins. / Imai, Takayoshi; Yagi, Yusuke; Nakamura, Takahiro.

Applied RNA Bioscience. Springer Singapore, 2018. p. 151-160.

Research output: Chapter in Book/Report/Conference proceedingChapter

Imai, Takayoshi ; Yagi, Yusuke ; Nakamura, Takahiro. / Recent progress toward RNA manipulation with engineered pentatricopeptide repeat proteins. Applied RNA Bioscience. Springer Singapore, 2018. pp. 151-160
@inbook{a56bfe99d550439d924cfbbd87050653,
title = "Recent progress toward RNA manipulation with engineered pentatricopeptide repeat proteins",
abstract = "Pentatricopeptide repeat (PPR) proteins are RNA-binding proteins that are widely distributed in plants. They contain 2 to 30 repeating units of ~35-amino acid PPR motifs. They are known to play important roles in RNA processing, RNA editing, and translational regulation. Recent studies on the RNA recognition mode of PPR proteins revealed that one PPR motif interacts with one nucleotide. In addition, it was revealed that amino acids at three specific positions in a single motif serve to specify its binding base. Thus, mutation of these amino acids can cause a modification of the binding specificity of PPR motifs. Indeed, the engineered PPR motifs fused with various effector domains are shown to bind to and manipulate RNAs in a controlled manner. In this review, we summarize the recent progress in structural studies on PPR motifs. We focus on their RNA recognition mode and discuss the potentials of PPR as novel, versatile tools for RNA manipulation.",
author = "Takayoshi Imai and Yusuke Yagi and Takahiro Nakamura",
year = "2018",
month = "4",
day = "10",
doi = "10.1007/978-981-10-8372-3_10",
language = "English",
isbn = "9789811083716",
pages = "151--160",
booktitle = "Applied RNA Bioscience",
publisher = "Springer Singapore",

}

TY - CHAP

T1 - Recent progress toward RNA manipulation with engineered pentatricopeptide repeat proteins

AU - Imai, Takayoshi

AU - Yagi, Yusuke

AU - Nakamura, Takahiro

PY - 2018/4/10

Y1 - 2018/4/10

N2 - Pentatricopeptide repeat (PPR) proteins are RNA-binding proteins that are widely distributed in plants. They contain 2 to 30 repeating units of ~35-amino acid PPR motifs. They are known to play important roles in RNA processing, RNA editing, and translational regulation. Recent studies on the RNA recognition mode of PPR proteins revealed that one PPR motif interacts with one nucleotide. In addition, it was revealed that amino acids at three specific positions in a single motif serve to specify its binding base. Thus, mutation of these amino acids can cause a modification of the binding specificity of PPR motifs. Indeed, the engineered PPR motifs fused with various effector domains are shown to bind to and manipulate RNAs in a controlled manner. In this review, we summarize the recent progress in structural studies on PPR motifs. We focus on their RNA recognition mode and discuss the potentials of PPR as novel, versatile tools for RNA manipulation.

AB - Pentatricopeptide repeat (PPR) proteins are RNA-binding proteins that are widely distributed in plants. They contain 2 to 30 repeating units of ~35-amino acid PPR motifs. They are known to play important roles in RNA processing, RNA editing, and translational regulation. Recent studies on the RNA recognition mode of PPR proteins revealed that one PPR motif interacts with one nucleotide. In addition, it was revealed that amino acids at three specific positions in a single motif serve to specify its binding base. Thus, mutation of these amino acids can cause a modification of the binding specificity of PPR motifs. Indeed, the engineered PPR motifs fused with various effector domains are shown to bind to and manipulate RNAs in a controlled manner. In this review, we summarize the recent progress in structural studies on PPR motifs. We focus on their RNA recognition mode and discuss the potentials of PPR as novel, versatile tools for RNA manipulation.

UR - http://www.scopus.com/inward/record.url?scp=85053950067&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85053950067&partnerID=8YFLogxK

U2 - 10.1007/978-981-10-8372-3_10

DO - 10.1007/978-981-10-8372-3_10

M3 - Chapter

AN - SCOPUS:85053950067

SN - 9789811083716

SP - 151

EP - 160

BT - Applied RNA Bioscience

PB - Springer Singapore

ER -