| Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation. | |
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MedLine Citation:
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PMID: 17082182 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Spindlin1, a meiotic spindle-binding protein that is highly expressed in ovarian cancer cells, was first identified as a gene involved in gametogenesis. It appeared to be a target for cell cycle-dependent phosphorylation and was demonstrated to disturb the cell cycle. Here we report the crystal structure of human spindlin1 to 2.2A of resolution, representing the first three-dimensional structure from the spin/ssty (Y-linked spermiogenesis-specific transcript) gene family. The refined structure, containing three repeats of five/four anti-parallel beta-strands, exhibits a novel arrangement of tandem Tudor-like domains. Two phosphate ions, chelated by Thr-95 and other residues, appear to stabilize the long loop between domains I and II, which might mediate the cell cycle regulation activity of spindlin1. Flow cytometry experiments indicate that cells expressing spindlin1 display a different cell cycle distribution in mitosis, whereas those expressing a T95A mutant, which had a great decrease in phosphorous content, have little effect on the cell cycle. We further identified associations of spindlin1 with nucleic acid to provide a biochemical basis for its cell cycle regulation and other functions. |
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Authors:
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Qiang Zhao; Lipeng Qin; Fuguo Jiang; Beili Wu; Wen Yue; Feng Xu; Zhili Rong; Hongfeng Yuan; Xiaoyan Xie; Yanhong Gao; Cixian Bai; Mark Bartlam; Xuetao Pei; Zihe Rao |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2006-11-01 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 282 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2007 Jan |
Date Detail:
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Created Date: 2007-01-01 Completed Date: 2007-02-08 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 647-56 Citation Subset: IM |
Affiliation:
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Tsinghua-Institute of Biophysics Joint Research Group for Structural Biology, Tsinghua University, Beijing 100084, China. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/2NS2 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Cell Cycle Proteins / chemistry* Cell Line, Tumor Chelating Agents / pharmacology Crystallography, X-Ray Dimerization Humans Ions Microtubule-Associated Proteins / chemistry* Models, Molecular Molecular Sequence Data Phosphates / chemistry Phosphoproteins / chemistry* Phosphorylation Protein Structure, Tertiary Sequence Homology, Amino Acid Threonine / chemistry |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Chelating Agents; 0/Ions; 0/Microtubule-Associated Proteins; 0/Phosphates; 0/Phosphoproteins; 0/spindlin; 72-19-5/Threonine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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