Structural Characterization of RNA Recognition Motif-2 Domain of SART3

Kyeong Mi Bang; Na Youn Cho; Won Je Kim; Ae Ryung Kim; Hyun Kyu Song; Eunice Eun Kyeong Kim; Nak Kyoon Kim

doi:10.1002/bkcs.11106

Structural Characterization of RNA Recognition Motif-2 Domain of SART3

Kyeong Mi Bang, Na Youn Cho, Won Je Kim, Ae Ryung Kim, Hyun Kyu Song, Eunice Eun Kyeong Kim, Nak Kyoon Kim

Department of Life Sciences

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

Abstract

Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is an essential recycling factor in pre-mRNA splicing, which is required for association of U4/U6 small nuclear ribonucleoprotein (snRNP). SART3 contains two RNA recognition motifs (RRMs), and they are responsible for the tertiary interaction with U6 small nuclear RNA. Despite the importance of structural studies for understanding complicate U4/U6 snRNP recycling mechanism, only a few of them have been performed for SART3. Here, the structure of SART3 RRM2 was characterized by heteronuclear multi-dimensional nuclear magnetic resonance experiments. Nearly complete ¹H, ¹⁵N, and ¹³C chemical shifts of the backbone residues of RRM2 were assigned. In addition, the secondary structure of RRM2 were predicted by the chemical shift index and TALOS+ analyses, and the results showed that RRM2 forms a “β₁-α₁-β₂-β₃-α₂-β₄-β₅” structure, where β₄ is not common in the canonical RRM domain structures. Our results will provide structural basis for investigation of SART3-mediated U4/U6 snRNP complex formation.

Original language	English
Pages (from-to)	444-447
Number of pages	4
Journal	Bulletin of the Korean Chemical Society
Volume	38
Issue number	4
DOIs	https://doi.org/10.1002/bkcs.11106
Publication status	Published - 2017 Apr 1

Keywords

Nuclear magnetic resonance
RNA recognition motifs
Splicing
Squamous cell carcinoma antigen recognized by T-cells 3
Structure

ASJC Scopus subject areas

Chemistry(all)

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10.1002/bkcs.11106

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@article{c0dd71d171d743b6be8258e9aa767a44,

title = "Structural Characterization of RNA Recognition Motif-2 Domain of SART3",

abstract = "Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is an essential recycling factor in pre-mRNA splicing, which is required for association of U4/U6 small nuclear ribonucleoprotein (snRNP). SART3 contains two RNA recognition motifs (RRMs), and they are responsible for the tertiary interaction with U6 small nuclear RNA. Despite the importance of structural studies for understanding complicate U4/U6 snRNP recycling mechanism, only a few of them have been performed for SART3. Here, the structure of SART3 RRM2 was characterized by heteronuclear multi-dimensional nuclear magnetic resonance experiments. Nearly complete 1H, 15N, and 13C chemical shifts of the backbone residues of RRM2 were assigned. In addition, the secondary structure of RRM2 were predicted by the chemical shift index and TALOS+ analyses, and the results showed that RRM2 forms a “β1-α1-β2-β3-α2-β4-β5” structure, where β4 is not common in the canonical RRM domain structures. Our results will provide structural basis for investigation of SART3-mediated U4/U6 snRNP complex formation.",

keywords = "Nuclear magnetic resonance, RNA recognition motifs, Splicing, Squamous cell carcinoma antigen recognized by T-cells 3, Structure",

author = "Bang, {Kyeong Mi} and Cho, {Na Youn} and Kim, {Won Je} and Kim, {Ae Ryung} and Song, {Hyun Kyu} and Kim, {Eunice Eun Kyeong} and Kim, {Nak Kyoon}",

note = "Funding Information: This study was supported financially by the National Research Foundation of Korea (NRF) (2015R1A2A2A04005596 to N.-K.K), and Korea Institute of Science and Technology (2V04611 to N.-K.K). We thank to Korea Basic Science Institute (KBSI) for using their NMR spectroscopy.",

year = "2017",

month = apr,

day = "1",

doi = "10.1002/bkcs.11106",

language = "English",

volume = "38",

pages = "444--447",

journal = "Bulletin of the Korean Chemical Society",

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publisher = "Wiley-Blackwell",

number = "4",

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TY - JOUR

T1 - Structural Characterization of RNA Recognition Motif-2 Domain of SART3

AU - Bang, Kyeong Mi

AU - Cho, Na Youn

AU - Kim, Won Je

AU - Kim, Ae Ryung

AU - Song, Hyun Kyu

AU - Kim, Eunice Eun Kyeong

AU - Kim, Nak Kyoon

N1 - Funding Information: This study was supported financially by the National Research Foundation of Korea (NRF) (2015R1A2A2A04005596 to N.-K.K), and Korea Institute of Science and Technology (2V04611 to N.-K.K). We thank to Korea Basic Science Institute (KBSI) for using their NMR spectroscopy.

PY - 2017/4/1

Y1 - 2017/4/1

N2 - Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is an essential recycling factor in pre-mRNA splicing, which is required for association of U4/U6 small nuclear ribonucleoprotein (snRNP). SART3 contains two RNA recognition motifs (RRMs), and they are responsible for the tertiary interaction with U6 small nuclear RNA. Despite the importance of structural studies for understanding complicate U4/U6 snRNP recycling mechanism, only a few of them have been performed for SART3. Here, the structure of SART3 RRM2 was characterized by heteronuclear multi-dimensional nuclear magnetic resonance experiments. Nearly complete 1H, 15N, and 13C chemical shifts of the backbone residues of RRM2 were assigned. In addition, the secondary structure of RRM2 were predicted by the chemical shift index and TALOS+ analyses, and the results showed that RRM2 forms a “β1-α1-β2-β3-α2-β4-β5” structure, where β4 is not common in the canonical RRM domain structures. Our results will provide structural basis for investigation of SART3-mediated U4/U6 snRNP complex formation.

AB - Squamous cell carcinoma antigen recognized by T-cells 3 (SART3) is an essential recycling factor in pre-mRNA splicing, which is required for association of U4/U6 small nuclear ribonucleoprotein (snRNP). SART3 contains two RNA recognition motifs (RRMs), and they are responsible for the tertiary interaction with U6 small nuclear RNA. Despite the importance of structural studies for understanding complicate U4/U6 snRNP recycling mechanism, only a few of them have been performed for SART3. Here, the structure of SART3 RRM2 was characterized by heteronuclear multi-dimensional nuclear magnetic resonance experiments. Nearly complete 1H, 15N, and 13C chemical shifts of the backbone residues of RRM2 were assigned. In addition, the secondary structure of RRM2 were predicted by the chemical shift index and TALOS+ analyses, and the results showed that RRM2 forms a “β1-α1-β2-β3-α2-β4-β5” structure, where β4 is not common in the canonical RRM domain structures. Our results will provide structural basis for investigation of SART3-mediated U4/U6 snRNP complex formation.

KW - Nuclear magnetic resonance

KW - RNA recognition motifs

KW - Splicing

KW - Squamous cell carcinoma antigen recognized by T-cells 3

KW - Structure

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JO - Bulletin of the Korean Chemical Society

JF - Bulletin of the Korean Chemical Society

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Structural Characterization of RNA Recognition Motif-2 Domain of SART3

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Keywords

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