Genetic Evidence that the RAG1 Protein Directly Participates in V(D)J Recombination through Substrate Recognition
RAG1 protein is essential for the activation of V(D)J recombination in developing lymphocytes (V, variable; D, diversity; J, joining). However, it has not been determined whether its role involves substrate recognition and catalysis. A single amino acid substitution mutation in the RAG1 gene has now...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-03, Vol.93 (6), p.2333-2338 |
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description | RAG1 protein is essential for the activation of V(D)J recombination in developing lymphocytes (V, variable; D, diversity; J, joining). However, it has not been determined whether its role involves substrate recognition and catalysis. A single amino acid substitution mutation in the RAG1 gene has now been identified that renders its activity sensitive to the sequence of the coding region abutting the heptamer site in the recombination signal sequence. These results strongly imply that RAG1 interacts directly with DNA. |
doi_str_mv | 10.1073/pnas.93.6.2333 |
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These results strongly imply that RAG1 interacts directly with DNA.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.6.2333</identifier><identifier>PMID: 8637873</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Alleles ; Base Sequence ; Cell lines ; Cells, Cultured ; Deoxyribonucleic acid ; DNA ; Gene Rearrangement, B-Lymphocyte ; Genes, Immunoglobulin ; Genetic mutation ; Genetics ; Homeodomain Proteins ; Humans ; Lymphocytes ; Mice ; Molecular Sequence Data ; Nucleotides ; Oligodeoxyribonucleotides - chemistry ; Plasmids ; Polymerase chain reaction ; Proteins ; Proteins - metabolism ; Recombination, Genetic ; Substrate Specificity ; Transfection</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-03, Vol.93 (6), p.2333-2338</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Mar 19, 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c513t-6c054942011b01db0b8ab46e4d9dc35396365ed2c2ed5272f2094e988dffa5fd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/6.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/38673$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/38673$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27926,27927,53793,53795,58019,58252</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8637873$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Christopher A. 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These results strongly imply that RAG1 interacts directly with DNA.</description><subject>Alleles</subject><subject>Base Sequence</subject><subject>Cell lines</subject><subject>Cells, Cultured</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Gene Rearrangement, B-Lymphocyte</subject><subject>Genes, Immunoglobulin</subject><subject>Genetic mutation</subject><subject>Genetics</subject><subject>Homeodomain Proteins</subject><subject>Humans</subject><subject>Lymphocytes</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nucleotides</subject><subject>Oligodeoxyribonucleotides - chemistry</subject><subject>Plasmids</subject><subject>Polymerase chain reaction</subject><subject>Proteins</subject><subject>Proteins - metabolism</subject><subject>Recombination, Genetic</subject><subject>Substrate Specificity</subject><subject>Transfection</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9v0zAcxS0EGqVw5YCEFHFAcEiw48SxpV2mbRTQJKbx42o5zjetq9TubGdi_z0OLVVBSFzsw_u8r9_XD6HnBBcEN_Td1qpQCFqwoqSUPkAzggXJWSXwQzTDuGxyXpXVY_QkhDXGWNQcn6ATzmjDGzpDtwuwEI3OLu9MB1ZDFlcqpgOym7MFya69i2BsdmE86DjcZ9fKJ9xsVYSQJeH7m4u3n7Ib0G7TGquicTa5vRuXq-zL2IboE_lLX1ozqU_Ro14NAZ7t7zn69v7y6_mH_Orz4uP52VWua0JjzjSuK1GVmJAWk67FLVdtxaDqRKdpTQWjrIau1CV0ddmUfYlFBYLzru9V3Xd0jk53c7dju4FOg01RBrn1ZqP8vXTKyD8Va1Zy6e4kFU0aPkev93bvbkcIUW5M0DAMyoIbg2waIXhN8H9BUrPUCCMJfPUXuHajt-kPZNqyIpykBueo2EHauxA89IfABMupcDkVLgWVTE6FJ8PL4zUP-L7ho3iT77d68Mt-HIYIP-LRoH-CSX-x09chOn8AKGfplZ8aVsh9</recordid><startdate>19960319</startdate><enddate>19960319</enddate><creator>Christopher A. 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A single amino acid substitution mutation in the RAG1 gene has now been identified that renders its activity sensitive to the sequence of the coding region abutting the heptamer site in the recombination signal sequence. These results strongly imply that RAG1 interacts directly with DNA.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8637873</pmid><doi>10.1073/pnas.93.6.2333</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Alleles Base Sequence Cell lines Cells, Cultured Deoxyribonucleic acid DNA Gene Rearrangement, B-Lymphocyte Genes, Immunoglobulin Genetic mutation Genetics Homeodomain Proteins Humans Lymphocytes Mice Molecular Sequence Data Nucleotides Oligodeoxyribonucleotides - chemistry Plasmids Polymerase chain reaction Proteins Proteins - metabolism Recombination, Genetic Substrate Specificity Transfection |
title | Genetic Evidence that the RAG1 Protein Directly Participates in V(D)J Recombination through Substrate Recognition |
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