Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
25 01 2022
Historique:
accepted: 17 11 2021
entrez: 21 1 2022
pubmed: 22 1 2022
medline: 1 3 2022
Statut: ppublish

Résumé

Pseudouridine (Ψ) is a ubiquitous RNA modification incorporated by pseudouridine synthase (Pus) enzymes into hundreds of noncoding and protein-coding RNA substrates. Here, we determined the contributions of substrate structure and protein sequence to binding and catalysis by pseudouridine synthase 7 (Pus7), one of the principal messenger RNA (mRNA) modifying enzymes. Pus7 is distinct among the eukaryotic Pus proteins because it modifies a wider variety of substrates and shares limited homology with other Pus family members. We solved the crystal structure of

Identifiants

pubmed: 35058356
pii: 2109708119
doi: 10.1073/pnas.2109708119
pmc: PMC8794802
pii:
doi:

Substances chimiques

Pus7 protein, S cerevisiae 0
RNA, Fungal 0
RNA, Messenger 0
Saccharomyces cerevisiae Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : T32 GM132046
Pays : United States

Informations de copyright

Copyright © 2022 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Meredith K Purchal (MK)

Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109.

Daniel E Eyler (DE)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Mehmet Tardu (M)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Monika K Franco (MK)

Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109.

Megan M Korn (MM)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Taslima Khan (T)

Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109.

Ryan McNassor (R)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Rachel Giles (R)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Katherine Lev (K)

Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109.

Hari Sharma (H)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Jeremy Monroe (J)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

Leena Mallik (L)

Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.
Department of Biophysics, University of Michigan, Ann Arbor, MI 48109.

Markos Koutmos (M)

Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109; mkoutmos@umich.edu kkoutmou@umich.edu.
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.
Department of Biophysics, University of Michigan, Ann Arbor, MI 48109.

Kristin S Koutmou (KS)

Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109; mkoutmos@umich.edu kkoutmou@umich.edu.
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109.

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Classifications MeSH