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Title: Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8

The structure of the complex of NO66 and Rpl8 was solved in the native state and NO66 recognizes the consensus motif NHXH . Tetramerization is required for efficient substrate binding and catalysis by NO66. The JmjC domain-containing proteins belong to a large family of oxygenases possessing distinct substrate specificities which are involved in the regulation of different biological processes, such as gene transcription, RNA processing and translation. Nucleolar protein 66 (NO66) is a JmjC domain-containing protein which has been reported to be a histone demethylase and a ribosome protein 8 (Rpl8) hydroxylase. The present biochemical study confirmed the hydroxylase activity of NO66 and showed that oligomerization is required for NO66 to efficiently catalyze the hydroxylation of Rpl8. The structures of NO66{sup 176–C} complexed with Rpl8{sup 204–224} in a tetrameric form and of the mutant protein M2 in a dimeric form were solved. Based on the results of structural and biochemical analyses, the consensus sequence motif NHXH recognized by NO66 was confirmed. Several potential substrates of NO66 were found by a BLAST search according to the consensus sequence motif. When binding to substrate, the relative positions of each subunit in the NO66 tetramer shift. Oligomerization may facilitate the motion of eachmore » subunit in the NO66 tetramer and affect the catalytic activity.« less
Authors:
 [1] ;  [2] ;  [1] ;  [1] ;  [2] ;  [3] ;  [1] ; ; ;  [1] ;  [2]
  1. University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People’s Republic of (China)
  2. (China)
  3. Shanghai Children’s Medical Center, 1678 Dongfang Road, Pudong, Shanghai 200120, People’s Republic of (China)
Publication Date:
OSTI Identifier:
22425424
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 71; Journal Issue: Pt 9; Other Information: PMCID: PMC4556315; PMID: 26327385; PUBLISHER-ID: qh5028; OAI: oai:pubmedcentral.nih.gov:4556315; Copyright (c) Wang et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; 36 MATERIALS SCIENCE; EXPLOSIONS; MOLECULAR STRUCTURE; PROTEINS; SUBSTRATES