Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine

Abstract Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Ψ1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger me...

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Autores principales:	Cha San Koh, Rohini Madireddy, Timothy J. Beane, Phillip D. Zamore, Andrei A. Korostelev
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d054ded6d21e412c86951938f4ea5fff
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spelling	oai:doaj.org-article:d054ded6d21e412c86951938f4ea5fff2021-12-02T12:30:13ZSmall methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine10.1038/s41598-017-01186-52045-2322https://doaj.org/article/d054ded6d21e412c86951938f4ea5fff2017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01186-5https://doaj.org/toc/2045-2322Abstract Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Ψ1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture.Cha San KohRohini MadireddyTimothy J. BeanePhillip D. ZamoreAndrei A. KorostelevNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Cha San Koh Rohini Madireddy Timothy J. Beane Phillip D. Zamore Andrei A. Korostelev Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
description	Abstract Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Ψ1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture.
format	article
author	Cha San Koh Rohini Madireddy Timothy J. Beane Phillip D. Zamore Andrei A. Korostelev
author_facet	Cha San Koh Rohini Madireddy Timothy J. Beane Phillip D. Zamore Andrei A. Korostelev
author_sort	Cha San Koh
title	Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
title_short	Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
title_full	Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
title_fullStr	Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
title_full_unstemmed	Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine
title_sort	small methyltransferase rlmh assembles a composite active site to methylate a ribosomal pseudouridine
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d054ded6d21e412c86951938f4ea5fff
work_keys_str_mv	AT chasankoh smallmethyltransferaserlmhassemblesacompositeactivesitetomethylatearibosomalpseudouridine AT rohinimadireddy smallmethyltransferaserlmhassemblesacompositeactivesitetomethylatearibosomalpseudouridine AT timothyjbeane smallmethyltransferaserlmhassemblesacompositeactivesitetomethylatearibosomalpseudouridine AT phillipdzamore smallmethyltransferaserlmhassemblesacompositeactivesitetomethylatearibosomalpseudouridine AT andreiakorostelev smallmethyltransferaserlmhassemblesacompositeactivesitetomethylatearibosomalpseudouridine
_version_	1718394426619854848

Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine

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