Stability of mutant actins
Mutants of the Drosophila Act88F actin gene were transcribed and translated in vitro and their relative stabilities were examined using urea gradient gel electrophoresis. Most of the mutant actins (E334K, E364K, G366D, G368E and R372H) were as stable as the wild-type. V339I had a slight decrease in...
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| Veröffentlicht in: | Biochemical journal 1991-02, Vol.274 (1), p.301-303 |
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| container_title | Biochemical journal |
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| creator | Drummond, D.D Hennessey, E.S Sparrow, J.C |
| description | Mutants of the Drosophila Act88F actin gene were transcribed and translated in vitro and their relative stabilities were examined using urea gradient gel electrophoresis. Most of the mutant actins (E334K, E364K, G366D, G368E and R372H) were as stable as the wild-type. V339I had a slight decrease in stability, and E316K was the least stable. The causes of the differences are discussed and contrasted with the behaviour of the mutants in vivo, where E316K has normal stability and V339I is the least stable. |
| doi_str_mv | 10.1042/bj2740301 |
| format | Article |
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Most of the mutant actins (E334K, E364K, G366D, G368E and R372H) were as stable as the wild-type. V339I had a slight decrease in stability, and E316K was the least stable. The causes of the differences are discussed and contrasted with the behaviour of the mutants in vivo, where E316K has normal stability and V339I is the least stable.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2740301</identifier><identifier>PMID: 2001247</identifier><language>eng</language><publisher>Colchester: Portland Press</publisher><subject>actin ; Actins - chemistry ; Actins - genetics ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Contractile proteins ; Drosophila ; Drug Stability ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. 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Most of the mutant actins (E334K, E364K, G366D, G368E and R372H) were as stable as the wild-type. V339I had a slight decrease in stability, and E316K was the least stable. The causes of the differences are discussed and contrasted with the behaviour of the mutants in vivo, where E316K has normal stability and V339I is the least stable.</description><subject>actin</subject><subject>Actins - chemistry</subject><subject>Actins - genetics</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Contractile proteins</subject><subject>Drosophila</subject><subject>Drug Stability</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Holoproteins</subject><subject>mutants</subject><subject>Mutation</subject><subject>Protein Biosynthesis</subject><subject>Protein Denaturation</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>stability</subject><subject>transcription (genetics)</subject><subject>Transcription, Genetic</subject><subject>translation</subject><subject>Urea</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkM1Lw0AQxRdRaq0evApiLwoeojOTTZO9CFL8goKH2vMyySY1JR81mwj9711tqHoYZuD9ePN4Qpwi3CBIuo1XFErwAffEEGUIXhRStC-GQBPpTYDwUBxZuwJACRIGYkDuJBkOxdm85Tgv8nYzrrNx2bVctWNO2ryyx-Ig48KmJ_0eicXjw9v02Zu9Pr1M72deIkm2nsqAJCoffQOpkdIEYZwQRFLFhMqEBlExcKiMiaPMkIHMTazYRwhin_2RuNv6rru4TE2SVm3DhV43ecnNRtec6_9Klb_rZf2pEaVSge8MrnqDpv7oUtvqMrdJWhRcpXVndQRyogJCB15vwaSprW3SbPcEQX8XqXdFOvb8b6od2Tfn9MteZ5twkTVcJbn9NXTBAvkT7mLLZVxrXjaOWczJPQAKkchhX7KOgoQ</recordid><startdate>19910215</startdate><enddate>19910215</enddate><creator>Drummond, D.D</creator><creator>Hennessey, E.S</creator><creator>Sparrow, J.C</creator><general>Portland Press</general><scope>FBQ</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19910215</creationdate><title>Stability of mutant actins</title><author>Drummond, D.D ; Hennessey, E.S ; Sparrow, J.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c424t-9f02419313d0ed44d57bc20849b219d7d119a0a79ddb8fd2d0f2d0b9a3105b3a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>actin</topic><topic>Actins - chemistry</topic><topic>Actins - genetics</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Contractile proteins</topic><topic>Drosophila</topic><topic>Drug Stability</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Holoproteins</topic><topic>mutants</topic><topic>Mutation</topic><topic>Protein Biosynthesis</topic><topic>Protein Denaturation</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>stability</topic><topic>transcription (genetics)</topic><topic>Transcription, Genetic</topic><topic>translation</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Drummond, D.D</creatorcontrib><creatorcontrib>Hennessey, E.S</creatorcontrib><creatorcontrib>Sparrow, J.C</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Drummond, D.D</au><au>Hennessey, E.S</au><au>Sparrow, J.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stability of mutant actins</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1991-02-15</date><risdate>1991</risdate><volume>274</volume><issue>1</issue><spage>301</spage><epage>303</epage><pages>301-303</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Mutants of the Drosophila Act88F actin gene were transcribed and translated in vitro and their relative stabilities were examined using urea gradient gel electrophoresis. Most of the mutant actins (E334K, E364K, G366D, G368E and R372H) were as stable as the wild-type. V339I had a slight decrease in stability, and E316K was the least stable. The causes of the differences are discussed and contrasted with the behaviour of the mutants in vivo, where E316K has normal stability and V339I is the least stable.</abstract><cop>Colchester</cop><pub>Portland Press</pub><pmid>2001247</pmid><doi>10.1042/bj2740301</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1991-02, Vol.274 (1), p.301-303 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | actin Actins - chemistry Actins - genetics Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Contractile proteins Drosophila Drug Stability Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology genes Holoproteins mutants Mutation Protein Biosynthesis Protein Denaturation Proteins Rabbits stability transcription (genetics) Transcription, Genetic translation Urea |
| title | Stability of mutant actins |
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