Tus, an E. coli protein, contains mammalian nuclear targeting and exporting signals
Shuttling of proteins between nucleus and cytoplasm in mammalian cells is facilitated by the presence of nuclear localization signals (NLS) and nuclear export signals (NES), respectively. However, we have found that Tus, an E. coli replication fork arresting protein, contains separate sequences that...
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| creator | Kaczmarczyk, Stanislaw J Sitaraman, Kalavathy Hill, Thomas Hartley, James L Chatterjee, Deb K |
| description | Shuttling of proteins between nucleus and cytoplasm in mammalian cells is facilitated by the presence of nuclear localization signals (NLS) and nuclear export signals (NES), respectively. However, we have found that Tus, an E. coli replication fork arresting protein, contains separate sequences that function efficiently as NLS and NES in mammalian cell lines, as judged by cellular location of GFP-fusion proteins. The NLS was localized to a short stretch of 9 amino acids in the carboxy-terminus of Tus protein. Alterations of any of these basic amino acids almost completely abolished the nuclear targeting. The NES comprises a cluster of leucine/hydrophobic residues located within 21 amino acids at the amino terminus of Tus. Finally, we have shown that purified GFP-Tus fusion protein or GFP-Tus NLS fusion protein, when added to the culture media, was internalized very efficiently into mammalian cells. Thus, Tus is perhaps the first reported bacterial protein to possess both NLS and NES, and has the capability to transduce protein into mammalian cells. |
| doi_str_mv | 10.1371/journal.pone.0008889 |
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However, we have found that Tus, an E. coli replication fork arresting protein, contains separate sequences that function efficiently as NLS and NES in mammalian cell lines, as judged by cellular location of GFP-fusion proteins. The NLS was localized to a short stretch of 9 amino acids in the carboxy-terminus of Tus protein. Alterations of any of these basic amino acids almost completely abolished the nuclear targeting. The NES comprises a cluster of leucine/hydrophobic residues located within 21 amino acids at the amino terminus of Tus. Finally, we have shown that purified GFP-Tus fusion protein or GFP-Tus NLS fusion protein, when added to the culture media, was internalized very efficiently into mammalian cells. Thus, Tus is perhaps the first reported bacterial protein to possess both NLS and NES, and has the capability to transduce protein into mammalian cells.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0008889</identifier><identifier>PMID: 20126275</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Bacteria ; Base Sequence ; Biochemistry/Chemical Biology of the Cell ; Biochemistry/Drug Discovery ; Biochemistry/Molecular Evolution ; Biochemistry/Protein Chemistry ; Biotechnology/Protein Chemistry and Proteomics ; Cancer ; Cell Biology/Cell Growth and Division ; Cell Biology/Chemical Biology of the Cell ; Cell Biology/Gene Expression ; Cell culture ; Cell Line, Tumor ; Cell lines ; Cell Nucleus - metabolism ; Cells (Biology) ; Cloning ; Culture media ; Cytoplasm ; Deoxyribonucleic acid ; DNA ; DNA Primers ; E coli ; Escherichia coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Fusion protein ; Genetic engineering ; Genomes ; Humans ; Hydrocarbons ; Hydrophobicity ; International trade ; Laboratories ; Leucine ; Localization ; Male ; Mammalian cells ; Mammals ; Molecular Sequence Data ; Nuclear Export Signals ; Nuclear transport ; Nuclei (cytology) ; Peptides ; Protein expression ; Proteins ; Sequences ; Trends</subject><ispartof>PloS one, 2010-01, Vol.5 (1), p.e8889-e8889</ispartof><rights>COPYRIGHT 2010 Public Library of Science</rights><rights>2010 Kaczmarczyk et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Kaczmarczyk et al. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-f1287f079353f6bbfb123c9c221760f1eb7bd87ff93639d46f51d01062bc74503</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811178/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811178/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20126275$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Romesberg, Floyd</contributor><creatorcontrib>Kaczmarczyk, Stanislaw J</creatorcontrib><creatorcontrib>Sitaraman, Kalavathy</creatorcontrib><creatorcontrib>Hill, Thomas</creatorcontrib><creatorcontrib>Hartley, James L</creatorcontrib><creatorcontrib>Chatterjee, Deb K</creatorcontrib><title>Tus, an E. coli protein, contains mammalian nuclear targeting and exporting signals</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Shuttling of proteins between nucleus and cytoplasm in mammalian cells is facilitated by the presence of nuclear localization signals (NLS) and nuclear export signals (NES), respectively. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kaczmarczyk, Stanislaw J</au><au>Sitaraman, Kalavathy</au><au>Hill, Thomas</au><au>Hartley, James L</au><au>Chatterjee, Deb K</au><au>Romesberg, Floyd</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tus, an E. coli protein, contains mammalian nuclear targeting and exporting signals</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2010-01-26</date><risdate>2010</risdate><volume>5</volume><issue>1</issue><spage>e8889</spage><epage>e8889</epage><pages>e8889-e8889</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Shuttling of proteins between nucleus and cytoplasm in mammalian cells is facilitated by the presence of nuclear localization signals (NLS) and nuclear export signals (NES), respectively. However, we have found that Tus, an E. coli replication fork arresting protein, contains separate sequences that function efficiently as NLS and NES in mammalian cell lines, as judged by cellular location of GFP-fusion proteins. The NLS was localized to a short stretch of 9 amino acids in the carboxy-terminus of Tus protein. Alterations of any of these basic amino acids almost completely abolished the nuclear targeting. The NES comprises a cluster of leucine/hydrophobic residues located within 21 amino acids at the amino terminus of Tus. Finally, we have shown that purified GFP-Tus fusion protein or GFP-Tus NLS fusion protein, when added to the culture media, was internalized very efficiently into mammalian cells. Thus, Tus is perhaps the first reported bacterial protein to possess both NLS and NES, and has the capability to transduce protein into mammalian cells.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>20126275</pmid><doi>10.1371/journal.pone.0008889</doi><tpages>e8889</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Bacteria Base Sequence Biochemistry/Chemical Biology of the Cell Biochemistry/Drug Discovery Biochemistry/Molecular Evolution Biochemistry/Protein Chemistry Biotechnology/Protein Chemistry and Proteomics Cancer Cell Biology/Cell Growth and Division Cell Biology/Chemical Biology of the Cell Cell Biology/Gene Expression Cell culture Cell Line, Tumor Cell lines Cell Nucleus - metabolism Cells (Biology) Cloning Culture media Cytoplasm Deoxyribonucleic acid DNA DNA Primers E coli Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Fusion protein Genetic engineering Genomes Humans Hydrocarbons Hydrophobicity International trade Laboratories Leucine Localization Male Mammalian cells Mammals Molecular Sequence Data Nuclear Export Signals Nuclear transport Nuclei (cytology) Peptides Protein expression Proteins Sequences Trends |
| title | Tus, an E. coli protein, contains mammalian nuclear targeting and exporting signals |
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