Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail

Abstract Eukaryotic mature mRNAs possess a poly adenylate tail (poly(A)), to which multiple molecules of poly(A)-binding protein C1 (PABPC1) bind. PABPC1 regulates translation and mRNA metabolism by binding to regulatory proteins. To understand functional mechanism of the regulatory proteins, it is...

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Autores principales:	Ryoichi Sawazaki, Shunsuke Imai, Mariko Yokogawa, Nao Hosoda, Shin-ichi Hoshino, Muneyo Mio, Kazuhiro Mio, Ichio Shimada, Masanori Osawa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/72a8c212de0b4c6b858a335b08566f8e
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spelling	oai:doaj.org-article:72a8c212de0b4c6b858a335b08566f8e2021-12-02T15:08:13ZCharacterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail10.1038/s41598-018-19659-62045-2322https://doaj.org/article/72a8c212de0b4c6b858a335b08566f8e2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-19659-6https://doaj.org/toc/2045-2322Abstract Eukaryotic mature mRNAs possess a poly adenylate tail (poly(A)), to which multiple molecules of poly(A)-binding protein C1 (PABPC1) bind. PABPC1 regulates translation and mRNA metabolism by binding to regulatory proteins. To understand functional mechanism of the regulatory proteins, it is necessary to reveal how multiple molecules of PABPC1 exist on poly(A). Here, we characterize the structure of the multiple molecules of PABPC1 on poly(A), by using transmission electron microscopy (TEM), chemical cross-linking, and NMR spectroscopy. The TEM images and chemical cross-linking results indicate that multiple PABPC1 molecules form a wormlike structure in the PABPC1-poly(A) complex, in which the PABPC1 molecules are linearly arrayed. NMR and cross-linking analyses indicate that PABPC1 forms a multimer by binding to the neighbouring PABPC1 molecules via interactions between the RNA recognition motif (RRM) 2 in one molecule and the middle portion of the linker region of another molecule. A PABPC1 mutant lacking the interaction site in the linker, which possesses an impaired ability to form the multimer, reduced the in vitro translation activity, suggesting the importance of PABPC1 multimer formation in the translation process. We therefore propose a model of the PABPC1 multimer that provides clues to comprehensively understand the regulation mechanism of mRNA translation.Ryoichi SawazakiShunsuke ImaiMariko YokogawaNao HosodaShin-ichi HoshinoMuneyo MioKazuhiro MioIchio ShimadaMasanori OsawaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ryoichi Sawazaki Shunsuke Imai Mariko Yokogawa Nao Hosoda Shin-ichi Hoshino Muneyo Mio Kazuhiro Mio Ichio Shimada Masanori Osawa Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail
description	Abstract Eukaryotic mature mRNAs possess a poly adenylate tail (poly(A)), to which multiple molecules of poly(A)-binding protein C1 (PABPC1) bind. PABPC1 regulates translation and mRNA metabolism by binding to regulatory proteins. To understand functional mechanism of the regulatory proteins, it is necessary to reveal how multiple molecules of PABPC1 exist on poly(A). Here, we characterize the structure of the multiple molecules of PABPC1 on poly(A), by using transmission electron microscopy (TEM), chemical cross-linking, and NMR spectroscopy. The TEM images and chemical cross-linking results indicate that multiple PABPC1 molecules form a wormlike structure in the PABPC1-poly(A) complex, in which the PABPC1 molecules are linearly arrayed. NMR and cross-linking analyses indicate that PABPC1 forms a multimer by binding to the neighbouring PABPC1 molecules via interactions between the RNA recognition motif (RRM) 2 in one molecule and the middle portion of the linker region of another molecule. A PABPC1 mutant lacking the interaction site in the linker, which possesses an impaired ability to form the multimer, reduced the in vitro translation activity, suggesting the importance of PABPC1 multimer formation in the translation process. We therefore propose a model of the PABPC1 multimer that provides clues to comprehensively understand the regulation mechanism of mRNA translation.
format	article
author	Ryoichi Sawazaki Shunsuke Imai Mariko Yokogawa Nao Hosoda Shin-ichi Hoshino Muneyo Mio Kazuhiro Mio Ichio Shimada Masanori Osawa
author_facet	Ryoichi Sawazaki Shunsuke Imai Mariko Yokogawa Nao Hosoda Shin-ichi Hoshino Muneyo Mio Kazuhiro Mio Ichio Shimada Masanori Osawa
author_sort	Ryoichi Sawazaki
title	Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail
title_short	Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail
title_full	Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail
title_fullStr	Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail
title_full_unstemmed	Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail
title_sort	characterization of the multimeric structure of poly(a)-binding protein on a poly(a) tail
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/72a8c212de0b4c6b858a335b08566f8e
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Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail

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