Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1

Scisung Chung; Mi Sun Kang; Dauren S. Alimbetov; Gil Im Mun; Na Oh Yunn; Yunjin Kim; Byung Gyu Kim; Minwoo Wie; Eun A. Lee; Jae Sun Ra; Jung Min Oh; Donghyun Lee; Keondo Lee; Jihan Kim; Seung Hyun Han; Kyong Tai Kim; Wan Kyun Chung; Ki Hyun Nam; Jaehyun Park; Byung Hoon Lee; Sunghoon Kim; Weixing Zhao; Sung Ho Ryu; Yun Sil Lee; Kyungjae Myung; Yunje Cho

doi:10.1038/s41467-022-34612-y

Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1

Scisung Chung, Mi Sun Kang, Dauren S. Alimbetov, Gil Im Mun, Na Oh Yunn, Yunjin Kim, Byung Gyu Kim, Minwoo Wie, Eun A. Lee, Jae Sun Ra, Jung Min Oh, Donghyun Lee, Keondo Lee, Jihan Kim, Seung Hyun Han, Kyong Tai Kim, Wan Kyun Chung, Ki Hyun Nam, Jaehyun Park, Byung Hoon LeeSunghoon Kim, Weixing Zhao, Sung Ho Ryu, Yun Sil Lee, Kyungjae Myung, Yunje Cho

Department of Biochemistry & Structural Biology

Producción científica: Article › revisión exhaustiva

7 Citas (Scopus)

Resumen

Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function.

Idioma original	English (US)
Número de artículo	6732
Publicación	Nature communications
Volumen	13
N.º	1
DOI	https://doi.org/10.1038/s41467-022-34612-y
Estado	Published - dic 2022

ASJC Scopus subject areas

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

Acceder al documento

10.1038/s41467-022-34612-y

Otros archivos y enlaces

Citar esto

Chung, S., Kang, M. S., Alimbetov, D. S., Mun, G. I., Yunn, N. O., Kim, Y., Kim, B. G., Wie, M., Lee, E. A., Ra, J. S., Oh, J. M., Lee, D., Lee, K., Kim, J., Han, S. H., Kim, K. T., Chung, W. K., Nam, K. H., Park, J., ... Cho, Y. (2022). Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1. Nature communications, 13(1), Artículo 6732. https://doi.org/10.1038/s41467-022-34612-y

Chung, S, Kang, MS, Alimbetov, DS, Mun, GI, Yunn, NO, Kim, Y, Kim, BG, Wie, M, Lee, EA, Ra, JS, Oh, JM, Lee, D, Lee, K, Kim, J, Han, SH, Kim, KT, Chung, WK, Nam, KH, Park, J, Lee, BH, Kim, S, Zhao, W, Ryu, SH, Lee, YS, Myung, K & Cho, Y 2022, 'Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1', Nature communications, vol. 13, n.º 1, 6732. https://doi.org/10.1038/s41467-022-34612-y

@article{4537df49622e4d28ad674195f8fef677,

title = "Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1",

abstract = "Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function.",

author = "Scisung Chung and Kang, {Mi Sun} and Alimbetov, {Dauren S.} and Mun, {Gil Im} and Yunn, {Na Oh} and Yunjin Kim and Kim, {Byung Gyu} and Minwoo Wie and Lee, {Eun A.} and Ra, {Jae Sun} and Oh, {Jung Min} and Donghyun Lee and Keondo Lee and Jihan Kim and Han, {Seung Hyun} and Kim, {Kyong Tai} and Chung, {Wan Kyun} and Nam, {Ki Hyun} and Jaehyun Park and Lee, {Byung Hoon} and Sunghoon Kim and Weixing Zhao and Ryu, {Sung Ho} and Lee, {Yun Sil} and Kyungjae Myung and Yunje Cho",

note = "Publisher Copyright: {\textcopyright} 2022, The Author(s).",

year = "2022",

month = dec,

doi = "10.1038/s41467-022-34612-y",

language = "English (US)",

volume = "13",

journal = "Nature communications",

issn = "2041-1723",

publisher = "Nature Research",

number = "1",

}

TY - JOUR

T1 - Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1

AU - Chung, Scisung

AU - Kang, Mi Sun

AU - Alimbetov, Dauren S.

AU - Mun, Gil Im

AU - Yunn, Na Oh

AU - Kim, Yunjin

AU - Kim, Byung Gyu

AU - Wie, Minwoo

AU - Lee, Eun A.

AU - Ra, Jae Sun

AU - Oh, Jung Min

AU - Lee, Donghyun

AU - Lee, Keondo

AU - Kim, Jihan

AU - Han, Seung Hyun

AU - Kim, Kyong Tai

AU - Chung, Wan Kyun

AU - Nam, Ki Hyun

AU - Park, Jaehyun

AU - Lee, Byung Hoon

AU - Kim, Sunghoon

AU - Zhao, Weixing

AU - Ryu, Sung Ho

AU - Lee, Yun Sil

AU - Myung, Kyungjae

AU - Cho, Yunje

PY - 2022/12

Y1 - 2022/12

N2 - Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function.

AB - Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function.

UR - http://www.scopus.com/inward/record.url?scp=85141589378&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85141589378&partnerID=8YFLogxK

U2 - 10.1038/s41467-022-34612-y

DO - 10.1038/s41467-022-34612-y

M3 - Article

C2 - 36347866

AN - SCOPUS:85141589378

SN - 2041-1723

VL - 13

JO - Nature communications

JF - Nature communications

IS - 1

M1 - 6732

ER -

Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1

Resumen

ASJC Scopus subject areas

Acceder al documento

Otros archivos y enlaces

Huella

Citar esto