دورية أكاديمية
A metabolic alkene reporter for spatiotemporally controlled imaging of newly synthesized proteins in Mammalian cells.
العنوان: | A metabolic alkene reporter for spatiotemporally controlled imaging of newly synthesized proteins in Mammalian cells. |
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المؤلفون: | Song W; Department of Chemistry, State University of New York at Buffalo, 14260, USA., Wang Y, Yu Z, Vera CI, Qu J, Lin Q |
المصدر: | ACS chemical biology [ACS Chem Biol] 2010 Sep 17; Vol. 5 (9), pp. 875-85. |
نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Washington, D.C. : American Chemical Society, c2006- |
مواضيع طبية MeSH: | Protein Biosynthesis*, Allylglycine/*analysis , Allylglycine/*metabolism , Proteins/*analysis , Proteins/*metabolism, Allylglycine/chemistry ; Amino Acid Sequence ; Animals ; Flow Cytometry ; HeLa Cells ; Humans ; Microscopy, Fluorescence ; Molecular Sequence Data ; Proteins/chemistry |
مستخلص: | The nonsymmetrical spatial distribution of newly synthesized proteins in animal cells plays a central role in many cellular processes. Here, we report that a simple alkene tag, homoallylglycine (HAG), was co-translationally incorporated into a recombinant protein as well as endogenous, newly synthesized proteins in mammalian cells with high efficiency. In conjunction with a photoinduced tetrazole-alkene cycloaddition reaction ("photoclick chemistry"), this alkene tag further served as a bioorthogonal chemical reporter both for the selective protein functionalization in vitro and for a spatiotemporally controlled imaging of the newly synthesized proteins in live mammalian cells. This two-step metabolic alkene tagging-photocontrolled chemical functionalization approach may offer a potentially useful tool to study the role of spatiotemporally regulated protein synthesis in mammalian cells. |
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معلومات مُعتمدة: | R01 GM085092 United States GM NIGMS NIH HHS; R01 GM085092-02 United States GM NIGMS NIH HHS; GM85092 United States GM NIGMS NIH HHS |
المشرفين على المادة: | 0 (Proteins) 1069-48-3 (Allylglycine) |
تواريخ الأحداث: | Date Created: 20100730 Date Completed: 20110118 Latest Revision: 20211020 |
رمز التحديث: | 20231215 |
مُعرف محوري في PubMed: | PMC2942984 |
DOI: | 10.1021/cb100193h |
PMID: | 20666508 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1554-8937 |
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DOI: | 10.1021/cb100193h |