APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic
Human APOBEC3G (hA3G) is a member of the APOBEC-1 related protein (ARP) family of cytidine deaminases. hA3G functions as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type 1 (HIV-1). Nothing is known about the cellula...
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Veröffentlicht in: | Biochemical and biophysical research communications 2006-11, Vol.350 (1), p.214-219 |
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creator | Bennett, Ryan P. Diner, Elie Sowden, Mark P. Lees, Joshua A. Wedekind, Joseph E. Smith, Harold C. |
description | Human APOBEC3G (hA3G) is a member of the APOBEC-1 related protein (ARP) family of cytidine deaminases. hA3G functions as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type 1 (HIV-1). Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. We demonstrate that hA3G is not a nucleo-cytoplasmic shuttling protein like APOBEC-1 and AID, but is strongly retained in the cytoplasm through a mechanism that involves both the N and C-terminal regions of the protein. |
doi_str_mv | 10.1016/j.bbrc.2006.09.032 |
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Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. 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Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. 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Diner, Elie ; Sowden, Mark P. ; Lees, Joshua A. ; Wedekind, Joseph E. ; Smith, Harold C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-9f84bdab2ebb8eaf6093b49bdf48c159eb92e21bd55934e6373a8ac5e7e9c01f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>AID</topic><topic>Amino Acid Sequence</topic><topic>APOBEC-1</topic><topic>APOBEC-1 Deaminase</topic><topic>APOBEC3G</topic><topic>Cell Nucleus - metabolism</topic><topic>Cytidine Deaminase - chemistry</topic><topic>Cytidine Deaminase - genetics</topic><topic>Cytidine Deaminase - metabolism</topic><topic>Cytoplasm - metabolism</topic><topic>HeLa Cells</topic><topic>Human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Leucine - genetics</topic><topic>Leucine - metabolism</topic><topic>Molecular Sequence Data</topic><topic>NES</topic><topic>NLS</topic><topic>Protein Transport</topic><topic>Retrovirus</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Trafficking</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bennett, Ryan P.</creatorcontrib><creatorcontrib>Diner, Elie</creatorcontrib><creatorcontrib>Sowden, Mark P.</creatorcontrib><creatorcontrib>Lees, Joshua A.</creatorcontrib><creatorcontrib>Wedekind, Joseph E.</creatorcontrib><creatorcontrib>Smith, Harold C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bennett, Ryan P.</au><au>Diner, Elie</au><au>Sowden, Mark P.</au><au>Lees, Joshua A.</au><au>Wedekind, Joseph E.</au><au>Smith, Harold C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-11-10</date><risdate>2006</risdate><volume>350</volume><issue>1</issue><spage>214</spage><epage>219</epage><pages>214-219</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Human APOBEC3G (hA3G) is a member of the APOBEC-1 related protein (ARP) family of cytidine deaminases. hA3G functions as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type 1 (HIV-1). Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. We demonstrate that hA3G is not a nucleo-cytoplasmic shuttling protein like APOBEC-1 and AID, but is strongly retained in the cytoplasm through a mechanism that involves both the N and C-terminal regions of the protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16999936</pmid><doi>10.1016/j.bbrc.2006.09.032</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | AID Amino Acid Sequence APOBEC-1 APOBEC-1 Deaminase APOBEC3G Cell Nucleus - metabolism Cytidine Deaminase - chemistry Cytidine Deaminase - genetics Cytidine Deaminase - metabolism Cytoplasm - metabolism HeLa Cells Human immunodeficiency virus 1 Humans Leucine - genetics Leucine - metabolism Molecular Sequence Data NES NLS Protein Transport Retrovirus Sequence Alignment Sequence Homology, Amino Acid Trafficking |
title | APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic |
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