Single polysome analysis of mRNP

Byungju Kim; Yeonkyoung Park; Hyun Jung Hwang; Jeeyoon Chang; Yoon Ki Kim; Jong Bong Lee

doi:10.1016/j.bbrc.2022.06.017

Single polysome analysis of mRNP

Byungju Kim, Yeonkyoung Park, Hyun Jung Hwang, Jeeyoon Chang, Yoon Ki Kim, Jong Bong Lee

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

Eukaryotic translation is a complex process that involves the interplay of various translation factors to convert genetic information into a specific amino acid chain. According to an elegant model of eukaryotic translation initiation, the 3′ poly(A) tail of an mRNA, which is occupied by poly(A)-binding proteins (PABPs), communicates with the 5′-cap bound by eIF4E to enhance translation. Although the circularization of mRNA resulting from the communication is widely understood, it has yet to be directly observed. To explore mRNA circularization in translation, we analyzed the level of colocalization of eIF4E, eIF4G, and PABP on individual mRNAs in polysomal and subpolysomal fractions using single polysome analysis. Our results show that the three tested proteins barely coexist in mRNA in either polysomal or subpolysomal fractions, implying that the closed-loop structure generated by the communication between eIF4E, eIF4G, and PAPB may be transient during translation.

Original language	English
Pages (from-to)	73-78
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	618
DOIs	https://doi.org/10.1016/j.bbrc.2022.06.017
Publication status	Published - 2022 Aug 27

Keywords

Closed-loop model
PABP(PABPC1)
Poly(A) tail
Polysome
Translation
mRNA

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2022.06.017

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title = "Single polysome analysis of mRNP",

abstract = "Eukaryotic translation is a complex process that involves the interplay of various translation factors to convert genetic information into a specific amino acid chain. According to an elegant model of eukaryotic translation initiation, the 3′ poly(A) tail of an mRNA, which is occupied by poly(A)-binding proteins (PABPs), communicates with the 5′-cap bound by eIF4E to enhance translation. Although the circularization of mRNA resulting from the communication is widely understood, it has yet to be directly observed. To explore mRNA circularization in translation, we analyzed the level of colocalization of eIF4E, eIF4G, and PABP on individual mRNAs in polysomal and subpolysomal fractions using single polysome analysis. Our results show that the three tested proteins barely coexist in mRNA in either polysomal or subpolysomal fractions, implying that the closed-loop structure generated by the communication between eIF4E, eIF4G, and PAPB may be transient during translation.",

keywords = "Closed-loop model, PABP(PABPC1), Poly(A) tail, Polysome, Translation, mRNA",

author = "Byungju Kim and Yeonkyoung Park and Hwang, {Hyun Jung} and Jeeyoon Chang and Kim, {Yoon Ki} and Lee, {Jong Bong}",

note = "Funding Information: The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Jong-Bong Lee reports financial support was provided by Korea Ministry of Science and ICT. Yoon Ki Kim reports financial support was provided by Korea Ministry of Science and ICT. Jong-Bong Lee reports a relationship with Korea Ministry of Science and ICT that includes: funding grants. Yoon Ki Kim reports a relationship with Korea Ministry of Science and ICT that includes: funding grants. Funding Information: This research was supported by the National Research Foundation of Korea funded by the Ministry of Science and ICT ( NRF-2015R1A3A2033665 to Y.K.K. and 2020R1A2C1012345 to J.B.L.). Publisher Copyright: {\textcopyright} 2022 The Authors",

year = "2022",

month = aug,

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doi = "10.1016/j.bbrc.2022.06.017",

language = "English",

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journal = "Biochemical and biophysical research communications",

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T1 - Single polysome analysis of mRNP

AU - Kim, Byungju

AU - Park, Yeonkyoung

AU - Hwang, Hyun Jung

AU - Chang, Jeeyoon

AU - Kim, Yoon Ki

AU - Lee, Jong Bong

N1 - Funding Information: The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Jong-Bong Lee reports financial support was provided by Korea Ministry of Science and ICT. Yoon Ki Kim reports financial support was provided by Korea Ministry of Science and ICT. Jong-Bong Lee reports a relationship with Korea Ministry of Science and ICT that includes: funding grants. Yoon Ki Kim reports a relationship with Korea Ministry of Science and ICT that includes: funding grants. Funding Information: This research was supported by the National Research Foundation of Korea funded by the Ministry of Science and ICT ( NRF-2015R1A3A2033665 to Y.K.K. and 2020R1A2C1012345 to J.B.L.). Publisher Copyright: © 2022 The Authors

PY - 2022/8/27

Y1 - 2022/8/27

N2 - Eukaryotic translation is a complex process that involves the interplay of various translation factors to convert genetic information into a specific amino acid chain. According to an elegant model of eukaryotic translation initiation, the 3′ poly(A) tail of an mRNA, which is occupied by poly(A)-binding proteins (PABPs), communicates with the 5′-cap bound by eIF4E to enhance translation. Although the circularization of mRNA resulting from the communication is widely understood, it has yet to be directly observed. To explore mRNA circularization in translation, we analyzed the level of colocalization of eIF4E, eIF4G, and PABP on individual mRNAs in polysomal and subpolysomal fractions using single polysome analysis. Our results show that the three tested proteins barely coexist in mRNA in either polysomal or subpolysomal fractions, implying that the closed-loop structure generated by the communication between eIF4E, eIF4G, and PAPB may be transient during translation.

AB - Eukaryotic translation is a complex process that involves the interplay of various translation factors to convert genetic information into a specific amino acid chain. According to an elegant model of eukaryotic translation initiation, the 3′ poly(A) tail of an mRNA, which is occupied by poly(A)-binding proteins (PABPs), communicates with the 5′-cap bound by eIF4E to enhance translation. Although the circularization of mRNA resulting from the communication is widely understood, it has yet to be directly observed. To explore mRNA circularization in translation, we analyzed the level of colocalization of eIF4E, eIF4G, and PABP on individual mRNAs in polysomal and subpolysomal fractions using single polysome analysis. Our results show that the three tested proteins barely coexist in mRNA in either polysomal or subpolysomal fractions, implying that the closed-loop structure generated by the communication between eIF4E, eIF4G, and PAPB may be transient during translation.

KW - Closed-loop model

KW - PABP(PABPC1)

KW - Poly(A) tail

KW - Polysome

KW - Translation

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JO - Biochemical and biophysical research communications

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ER -

Single polysome analysis of mRNP

Abstract

Keywords

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