Integration host factor: A protein for all reasons
The identification and characterization of the Escherichia coli DNA binding protein integration host factor (IHF) is an elegant example of how a well-characterized virus can be employed in the analysis of a host function. In this case, Nash and coworkers, through their landmark in vitro studies of c...
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| Veröffentlicht in: | Cell 1988-11, Vol.55 (4), p.545-554 |
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| creator | Friedman, David I. |
| description | The identification and characterization of the Escherichia coli DNA binding protein integration host factor (IHF) is an elegant example of how a well-characterized virus can be employed in the analysis of a host function. In this case, Nash and coworkers, through their landmark in vitro studies of coliphage lambda site-specific recombination, have identified a protein that plays roles not only in other recombination reactions, but also in DNA replication and regulation of gene expression. IHF belongs to a class of structurally related "histonelike" proteins that can wrap DNA into higher-order structures. The most abundant of these proteins in E. coli is HU, and others have been found in a number of bacterial genera as well as archaebacteria. In addition to site-specific recombination, other aspects of lambda development influenced by IHF have been fertile sources of information about this protein. The author initially focuses on studies with lambda that serve to present the basic information about IHF and then examine the various roles for IHF derived from studies of E. coli and some of its other phages and plasmids. |
| doi_str_mv | 10.1016/0092-8674(88)90213-9 |
| format | Article |
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In this case, Nash and coworkers, through their landmark in vitro studies of coliphage lambda site-specific recombination, have identified a protein that plays roles not only in other recombination reactions, but also in DNA replication and regulation of gene expression. IHF belongs to a class of structurally related "histonelike" proteins that can wrap DNA into higher-order structures. The most abundant of these proteins in E. coli is HU, and others have been found in a number of bacterial genera as well as archaebacteria. In addition to site-specific recombination, other aspects of lambda development influenced by IHF have been fertile sources of information about this protein. The author initially focuses on studies with lambda that serve to present the basic information about IHF and then examine the various roles for IHF derived from studies of E. coli and some of its other phages and plasmids.</description><subject>Bacterial Proteins - physiology</subject><subject>Bacteriophage lambda - enzymology</subject><subject>Bacteriophage lambda - genetics</subject><subject>Biological and medical sciences</subject><subject>DNA Nucleotidyltransferases - physiology</subject><subject>DNA Replication</subject><subject>DNA, Viral - biosynthesis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Genic rearrangement. Recombination. Transposable element</subject><subject>Integrases</subject><subject>Integration Host Factors</subject><subject>Lysogeny</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Structure</subject><subject>Molecular Weight</subject><subject>phage lambda</subject><subject>Recombination, Genetic</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEURYMotVb_gcIsRHQxmmQy-XAhlOJHoeBG1yHJJBqZTmqSCv57Z2zpUlcP3j3v8jgAnCJ4jSCiNxAKXHLKyCXnVwJiVJViD4wRFKwkiOF9MN4hh-AopQ8IIa_regRGWDBc8XoM8LzL9i2q7ENXvIeUC6dMDvG2mBarGLL1XeFCLFTbFtGqFLp0DA6capM92c4JeH24f5k9lYvnx_lsuihNjUUuGeKkFhoJwZnRGilmkFAMUc2wq7EjluGGkQohraFudL9ylBKNNGGNgqKagItNb__H59qmLJc-Gdu2qrNhnSTjhBNB_wdRjQkmlPcg2YAmhpSidXIV_VLFb4mgHJzKQZgchEnO5a9TOfSfbfvXemmb3dFWYp-fb3OVjGpdVJ3xaYdRxnrpsMfuNpjtpX15G2Uy3nbGNj5ak2UT_N9__ABDd5CD</recordid><startdate>19881118</startdate><enddate>19881118</enddate><creator>Friedman, David I.</creator><general>Elsevier Inc</general><general>Cell Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19881118</creationdate><title>Integration host factor: A protein for all reasons</title><author>Friedman, David I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c529t-718459b19987cbb1a7c19a716b72f52f4e72d74311bb0bdb52ff664b1b47da093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Bacterial Proteins - physiology</topic><topic>Bacteriophage lambda - enzymology</topic><topic>Bacteriophage lambda - genetics</topic><topic>Biological and medical sciences</topic><topic>DNA Nucleotidyltransferases - physiology</topic><topic>DNA Replication</topic><topic>DNA, Viral - biosynthesis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>Genic rearrangement. Recombination. Transposable element</topic><topic>Integrases</topic><topic>Integration Host Factors</topic><topic>Lysogeny</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Structure</topic><topic>Molecular Weight</topic><topic>phage lambda</topic><topic>Recombination, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Friedman, David I.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Friedman, David I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Integration host factor: A protein for all reasons</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1988-11-18</date><risdate>1988</risdate><volume>55</volume><issue>4</issue><spage>545</spage><epage>554</epage><pages>545-554</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>The identification and characterization of the Escherichia coli DNA binding protein integration host factor (IHF) is an elegant example of how a well-characterized virus can be employed in the analysis of a host function. In this case, Nash and coworkers, through their landmark in vitro studies of coliphage lambda site-specific recombination, have identified a protein that plays roles not only in other recombination reactions, but also in DNA replication and regulation of gene expression. IHF belongs to a class of structurally related "histonelike" proteins that can wrap DNA into higher-order structures. The most abundant of these proteins in E. coli is HU, and others have been found in a number of bacterial genera as well as archaebacteria. In addition to site-specific recombination, other aspects of lambda development influenced by IHF have been fertile sources of information about this protein. The author initially focuses on studies with lambda that serve to present the basic information about IHF and then examine the various roles for IHF derived from studies of E. coli and some of its other phages and plasmids.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>2972385</pmid><doi>10.1016/0092-8674(88)90213-9</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell, 1988-11, Vol.55 (4), p.545-554 |
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| subjects | Bacterial Proteins - physiology Bacteriophage lambda - enzymology Bacteriophage lambda - genetics Biological and medical sciences DNA Nucleotidyltransferases - physiology DNA Replication DNA, Viral - biosynthesis Fundamental and applied biological sciences. Psychology Gene Expression Regulation Genic rearrangement. Recombination. Transposable element Integrases Integration Host Factors Lysogeny Molecular and cellular biology Molecular genetics Molecular Structure Molecular Weight phage lambda Recombination, Genetic |
| title | Integration host factor: A protein for all reasons |
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