دورية أكاديمية
High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition.
| العنوان: | High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition. |
|---|---|
| المؤلفون: | Chiu YL; Gladstone Institute of Virology and Immunology, 1650 Owens Street, San Francisco, CA 94158, USA., Witkowska HE, Hall SC, Santiago M, Soros VB, Esnault C, Heidmann T, Greene WC |
| المصدر: | Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2006 Oct 17; Vol. 103 (42), pp. 15588-93. Date of Electronic Publication: 2006 Oct 09. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0027-8424 (Print) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, DC : National Academy of Sciences |
| مواضيع طبية MeSH: | Alu Elements* , Mutagenesis, Insertional*, Nucleoside Deaminases/*metabolism , Repressor Proteins/*metabolism, APOBEC-3G Deaminase ; Cell Line ; Cytidine Deaminase ; HIV-1/genetics ; HIV-1/metabolism ; Humans ; Macromolecular Substances ; Nucleic Acid Conformation ; Nucleoside Deaminases/chemistry ; RNA/genetics ; RNA/metabolism ; Repressor Proteins/chemistry ; Ribonucleoproteins/metabolism |
| مستخلص: | APOBEC3G (A3G) and related deoxycytidine deaminases are potent intrinsic antiretroviral factors. A3G is expressed either as an enzymatically active low-molecular-mass (LMM) form or as an enzymatically inactive high-molecular-mass (HMM) ribonucleoprotein complex. Resting CD4 T cells exclusively express LMM A3G, where it functions as a powerful postentry restriction factor for HIV-1. Activation of CD4 T cells promotes the recruitment of LMM A3G into 5- to 15-MDa HMM complexes whose function is unknown. Using tandem affinity purification techniques coupled with MS, we identified Staufen-containing RNA-transporting granules and Ro ribonucleoprotein complexes as specific components of HMM A3G complexes. Analysis of RNAs in these complexes revealed Alu and small Y RNAs, two of the most prominent nonautonomous mobile genetic elements in human cells. These retroelement RNAs are recruited into Staufen-containing RNA-transporting granules in the presence of A3G. Retrotransposition of Alu and hY RNAs depends on the reverse transcriptase machinery provided by long interspersed nucleotide elements 1 (L1). We now show that A3G greatly inhibits L1-dependent retrotransposition of marked Alu retroelements not by inhibiting L1 function but by sequestering Alu RNAs in cytoplasmic HMM A3G complexes away from the nuclear L1 enzymatic machinery. These findings identify nonautonomous Alu and hY retroelements as natural cellular targets of A3G and highlight how different forms of A3G uniquely protect cells from the threats posed by exogenous retroviruses (LMM A3G) and endogenous retroelements (HMM A3G). |
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| معلومات مُعتمدة: | R01 AI065329-01 United States AI NIAID NIH HHS; P01 HD040543 United States HD NICHD NIH HHS; RR18928-01 United States RR NCRR NIH HHS; P01 HD40543 United States HD NICHD NIH HHS; C06 RR018928 United States RR NCRR NIH HHS; R01 AI065329 United States AI NIAID NIH HHS |
| المشرفين على المادة: | 0 (Macromolecular Substances) 0 (Repressor Proteins) 0 (Ribonucleoproteins) 63231-63-0 (RNA) EC 3.5.4.- (Nucleoside Deaminases) EC 3.5.4.5 (APOBEC-3G Deaminase) EC 3.5.4.5 (APOBEC3G protein, human) EC 3.5.4.5 (Cytidine Deaminase) |
| تواريخ الأحداث: | Date Created: 20061013 Date Completed: 20070126 Latest Revision: 20181113 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC1592537 |
| DOI: | 10.1073/pnas.0604524103 |
| PMID: | 17030807 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0027-8424 |
|---|---|
| DOI: | 10.1073/pnas.0604524103 |