Characterization of the direct physical interaction of nc886, a cellular non-coding RNA, and PKR

Sung Ho Jeon; Kwanbok Lee; Kwang Soo Lee; Nawapol Kunkeaw; Betty H. Johnson; Luis Marcelo F. Holthauzen; Bin Gong; Chanvit Leelayuwat; Yong Sun Lee

doi:10.1016/j.febslet.2012.07.076

Characterization of the direct physical interaction of nc886, a cellular non-coding RNA, and PKR

Sung Ho Jeon, Kwanbok Lee, Kwang Soo Lee, Nawapol Kunkeaw, Betty H. Johnson, Luis Marcelo F. Holthauzen, Bin Gong, Chanvit Leelayuwat, Yong Sun Lee

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

55 Scopus citations

Abstract

We have recently shown that nc886 (pre-miR-886 or vtRNA2-1) is not a genuine microRNA precursor nor a vault RNA, but a novel type of non-coding RNA that represses PKR, a double-stranded RNA (dsRNA) dependent kinase. Here we have characterized their direct physical association. PKR's two RNA binding domains form a specific and stable complex with nc886's central portion, without any preference to its 5′-end structure. By binding to PKR with a comparable affinity, nc886 competes with dsRNA and attenuates PKR activation by dsRNA. Our data suggest that nc886 sets a threshold for PKR activation so that it occurs only during genuine viral infection but not by a minute level of fortuitous cellular dsRNA.

Original language	English (US)
Pages (from-to)	3477-3484
Number of pages	8
Journal	FEBS Letters
Volume	586
Issue number	19
DOIs	https://doi.org/10.1016/j.febslet.2012.07.076
State	Published - Sep 21 2012
Externally published	Yes

Keywords

Double-stranded RNA
PKR
Protein-RNA interaction
Vault RNA
nc886

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2012.07.076

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title = "Characterization of the direct physical interaction of nc886, a cellular non-coding RNA, and PKR",

abstract = "We have recently shown that nc886 (pre-miR-886 or vtRNA2-1) is not a genuine microRNA precursor nor a vault RNA, but a novel type of non-coding RNA that represses PKR, a double-stranded RNA (dsRNA) dependent kinase. Here we have characterized their direct physical association. PKR's two RNA binding domains form a specific and stable complex with nc886's central portion, without any preference to its 5′-end structure. By binding to PKR with a comparable affinity, nc886 competes with dsRNA and attenuates PKR activation by dsRNA. Our data suggest that nc886 sets a threshold for PKR activation so that it occurs only during genuine viral infection but not by a minute level of fortuitous cellular dsRNA.",

keywords = "Double-stranded RNA, PKR, Protein-RNA interaction, Vault RNA, nc886",

author = "Jeon, {Sung Ho} and Kwanbok Lee and Lee, {Kwang Soo} and Nawapol Kunkeaw and Johnson, {Betty H.} and Holthauzen, {Luis Marcelo F.} and Bin Gong and Chanvit Leelayuwat and Lee, {Yong Sun}",

note = "Funding Information: We thank Dr. Byung-Yoon Ahn of Korea University, Korea for plasmids. This work was supported by a Research Scholar Grant , RSG-12-187-01 – RMC from the American Cancer Society to YSL, by start-up funding from the Sealy Center for Cancer Biology at the University of Texas Medical Branch to YSL, and by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology ( 2011-0022022 ) and Hallym University Research Fund , 2011 ( HRF-2011–022 ) to SHJ. ",

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doi = "10.1016/j.febslet.2012.07.076",

language = "English (US)",

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AU - Jeon, Sung Ho

AU - Lee, Kwanbok

AU - Lee, Kwang Soo

AU - Kunkeaw, Nawapol

AU - Johnson, Betty H.

AU - Holthauzen, Luis Marcelo F.

AU - Gong, Bin

AU - Leelayuwat, Chanvit

AU - Lee, Yong Sun

N1 - Funding Information: We thank Dr. Byung-Yoon Ahn of Korea University, Korea for plasmids. This work was supported by a Research Scholar Grant , RSG-12-187-01 – RMC from the American Cancer Society to YSL, by start-up funding from the Sealy Center for Cancer Biology at the University of Texas Medical Branch to YSL, and by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology ( 2011-0022022 ) and Hallym University Research Fund , 2011 ( HRF-2011–022 ) to SHJ.

PY - 2012/9/21

Y1 - 2012/9/21

N2 - We have recently shown that nc886 (pre-miR-886 or vtRNA2-1) is not a genuine microRNA precursor nor a vault RNA, but a novel type of non-coding RNA that represses PKR, a double-stranded RNA (dsRNA) dependent kinase. Here we have characterized their direct physical association. PKR's two RNA binding domains form a specific and stable complex with nc886's central portion, without any preference to its 5′-end structure. By binding to PKR with a comparable affinity, nc886 competes with dsRNA and attenuates PKR activation by dsRNA. Our data suggest that nc886 sets a threshold for PKR activation so that it occurs only during genuine viral infection but not by a minute level of fortuitous cellular dsRNA.

AB - We have recently shown that nc886 (pre-miR-886 or vtRNA2-1) is not a genuine microRNA precursor nor a vault RNA, but a novel type of non-coding RNA that represses PKR, a double-stranded RNA (dsRNA) dependent kinase. Here we have characterized their direct physical association. PKR's two RNA binding domains form a specific and stable complex with nc886's central portion, without any preference to its 5′-end structure. By binding to PKR with a comparable affinity, nc886 competes with dsRNA and attenuates PKR activation by dsRNA. Our data suggest that nc886 sets a threshold for PKR activation so that it occurs only during genuine viral infection but not by a minute level of fortuitous cellular dsRNA.

KW - Double-stranded RNA

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KW - Protein-RNA interaction

KW - Vault RNA

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Characterization of the direct physical interaction of nc886, a cellular non-coding RNA, and PKR

Abstract

Keywords

ASJC Scopus subject areas

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