한빛사논문
- 조회896
Sohyun Gu1, Hyung-Min Jeon1, Seung Woo Nam1, Ka Young Hong1, Md Shafiqur Rahman1, Jong-Bong Lee2,3, Youngjin Kim1 and Sung Key Jang1,2,*
1Department of Life Sciences, Pohang University of Science and Technology, Nam-gu, Pohang 37673, Republic of Korea, 2School of Interdisciplinary Bioscience & Bioengineering, Pohang University of Science and Technology, Nam-gu, Pohang 37673, Republic of Korea and 3Department of Physices, Pohang University of Science and Technology, Nam-gu, Pohang 37673, Republic of Korea
*To whom correspondence should be addressed.
Abstract
Poly(A)-binding protein (PABP) is a translation initiation factor that interacts with the poly(A) tail of mRNAs. PABP bound to poly(A) stimulates translation by interacting with the eukaryotic initiation factor 4G (eIF4G), which brings the 3′ end of an mRNA close to its 5′ m7G cap structure through consecutive interactions of the 3′-poly(A)–PABP-eIF4G-eIF4E-5′ m7G cap. PABP is a highly abundant translation factor present in considerably larger quantities than mRNA and eIF4G in cells. However, it has not been elucidated how eIF4G, present in limited cellular concentrations, is not sequestered by mRNA-free PABP, present at high cellular concentrations, but associates with PABP complexed with the poly(A) tail of an mRNA. Here, we report that RNA-free PABPs dimerize with a head-to-head type configuration of PABP, which interferes in the interaction between PABP and eIF4G. We identified the domains of PABP responsible for PABP–PABP interaction. Poly(A) RNA was shown to convert the PABP–PABP complex into a poly(A)–PABP complex, with a head-to-tail-type configuration of PABP that facilitates the interaction between PABP and eIF4G. Lastly, we showed that the transition from the PABP dimer to the poly(A)–PABP complex is necessary for the translational activation function.
논문정보
- Research article
- 2021년 12월 (BRIC 등록일 2021-12-23)
- 국내 연구진
- 생명과학 > 감염생물학
댓글 작성 로그인
팝업 닫기관련 링크
연구자 키워드
연구자 ID
관련분야 연구자보기
소속기관 논문보기
관련분야 논문보기
해당논문 저자보기
