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Structural and functional insights into the human Upf1 helicase core.

Cheng Z, Muhlrad D, Lim MK, Parker R, Song H
EMBO J 26 253-64 (2007)
Related entries: 2gjk, 2gk7

Cited: 109 times
EuropePMC logo PMID: 17159905

Abstract

Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that recognizes and degrades aberrant mRNAs containing premature stop codons. A critical protein in NMD is Upf1p, which belongs to the helicase super family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to promote transitions in the structure of RNA or RNA-protein complexes. The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural comparison combined with mutational analysis identifies a likely single-stranded RNA (ssRNA)-binding channel, and a cycle of conformational change coupled to ATP binding and hydrolysis. These conformational changes alter the likely ssRNA-binding channel in a manner that can explain how ATP binding destabilizes ssRNA binding to Upf1p.

Articles - 2gk6 mentioned but not cited (8)

  1. Structural and functional insights into the human Upf1 helicase core. Cheng Z, Muhlrad D, Lim MK, Parker R, Song H. EMBO J 26 253-264 (2007)
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  6. Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex. Chen J, Wang Q, Malone B, Llewellyn E, Pechersky Y, Maruthi K, Eng ET, Perry JK, Campbell EA, Shaw DE, Darst SA. Nat Struct Mol Biol 29 250-260 (2022)
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  8. In Silico Analysis of the Structural and Biochemical Features of the NMD Factor UPF1 in Ustilago maydis. Martínez-Montiel N, Morales-Lara L, Hernández-Pérez JM, Martínez-Contreras RD. PLoS One 11 e0148191 (2016)


Reviews citing this publication (32)

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Articles citing this publication (69)

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