Document Detail


Structural basis for methylarginine-dependent recognition of Aubergine by Tudor.
MedLine Citation:
PMID:  20713507     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Piwi proteins are modified by symmetric dimethylation of arginine (sDMA), and the methylarginine-dependent interaction with Tudor domain proteins is critical for their functions in germline development. Cocrystal structures of an extended Tudor domain (eTud) of Drosophila Tudor with methylated peptides of Aubergine, a Piwi family protein, reveal that sDMA is recognized by an asparagine-gated aromatic cage. Furthermore, the unexpected Tudor-SN/p100 fold of eTud is important for sensing the position of sDMA. The structural information provides mechanistic insights into sDMA-dependent Piwi-Tudor interaction, and the recognition of sDMA by Tudor domains in general.
Authors:
Haiping Liu; Ju-Yu S Wang; Ying Huang; Zhizhong Li; Weimin Gong; Ruth Lehmann; Rui-Ming Xu
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-08-16
Journal Detail:
Title:  Genes & development     Volume:  24     ISSN:  1549-5477     ISO Abbreviation:  Genes Dev.     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-09-02     Completed Date:  2010-09-14     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  8711660     Medline TA:  Genes Dev     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1876-81     Citation Subset:  IM    
Affiliation:
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Arginine / analogs & derivatives*,  chemistry,  metabolism
Conserved Sequence
Drosophila Proteins / chemistry*,  metabolism*
Drosophila melanogaster / chemistry,  genetics,  metabolism*
Germ Cells / growth & development,  metabolism
Membrane Transport Proteins / chemistry*,  metabolism*
Models, Molecular*
Molecular Sequence Data
Peptide Initiation Factors / chemistry*,  metabolism*
Protein Binding
Protein Structure, Quaternary
Protein Structure, Tertiary
Sequence Alignment
Grant Support
ID/Acronym/Agency:
GM063716/GM/NIGMS NIH HHS; P30 EB009998/EB/NIBIB NIH HHS; //Howard Hughes Medical Institute; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Drosophila Proteins; 0/Membrane Transport Proteins; 0/Peptide Initiation Factors; 0/aubergine protein, Drosophila; 0/tud protein, Drosophila; 30344-00-4/N,N'-dimethylarginine; 74-79-3/Arginine
Comments/Corrections
Comment In:
Genes Dev. 2010 Sep 15;24(18):1963-6   [PMID:  20844011 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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