Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties
The GroEL molecular chaperone of Escherichia coli and its cofactor GroES are highly conserved, and are required for the folding of many proteins. Most but not all bacteria express single GroEL and GroES proteins. Rhizobium leguminosarum strain A34 encodes three complete operons encoding homologues t...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2004-11, Vol.324 (2), p.822-828 |
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| container_title | Biochemical and biophysical research communications |
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| creator | George, Roger Kelly, Sharon M. Price, Nicholas C. Erbse, Annette Fisher, Mark Lund, Peter A. |
| description | The GroEL molecular chaperone of Escherichia coli and its cofactor GroES are highly conserved, and are required for the folding of many proteins. Most but not all bacteria express single GroEL and GroES proteins. Rhizobium leguminosarum strain A34 encodes three complete operons encoding homologues to GroEL and GroES. We have used circular dichroism and measurement of ATPase activity to compare the stabilities of these chaperonins after expression in and purification from E. coli. Significant differences in the stabilities of the proteins with respect to denaturant and temperature were found. The proteins also differed in their ability to refold denatured lactate dehydrogenase. This study, the first to compare the properties of three different GroEL homologues from the same organism, shows that despite the high degree of similarity between different homologues, they can display distinct properties in vitro. |
| doi_str_mv | 10.1016/j.bbrc.2004.09.140 |
| format | Article |
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Most but not all bacteria express single GroEL and GroES proteins. Rhizobium leguminosarum strain A34 encodes three complete operons encoding homologues to GroEL and GroES. We have used circular dichroism and measurement of ATPase activity to compare the stabilities of these chaperonins after expression in and purification from E. coli. Significant differences in the stabilities of the proteins with respect to denaturant and temperature were found. The proteins also differed in their ability to refold denatured lactate dehydrogenase. 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Kelly, Sharon M. ; Price, Nicholas C. ; Erbse, Annette ; Fisher, Mark ; Lund, Peter A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c449t-31228b5952f46b9a5c727eed1819259d2a478afebadafaec78d88b83da27d4663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenosine Triphosphatases - chemistry</topic><topic>Cell Proliferation</topic><topic>Chaperonin</topic><topic>Chaperonin 60 - chemistry</topic><topic>Chaperonins - chemistry</topic><topic>Circular Dichroism</topic><topic>Cpn60</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>GroEL</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>L-Lactate Dehydrogenase - chemistry</topic><topic>L-Lactate Dehydrogenase - metabolism</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Rhizobium leguminosarum</topic><topic>Rhizobium leguminosarum - metabolism</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>George, Roger</creatorcontrib><creatorcontrib>Kelly, Sharon M.</creatorcontrib><creatorcontrib>Price, Nicholas C.</creatorcontrib><creatorcontrib>Erbse, Annette</creatorcontrib><creatorcontrib>Fisher, Mark</creatorcontrib><creatorcontrib>Lund, Peter A.</creatorcontrib><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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>George, Roger</au><au>Kelly, Sharon M.</au><au>Price, Nicholas C.</au><au>Erbse, Annette</au><au>Fisher, Mark</au><au>Lund, Peter A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2004-11-12</date><risdate>2004</risdate><volume>324</volume><issue>2</issue><spage>822</spage><epage>828</epage><pages>822-828</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The GroEL molecular chaperone of Escherichia coli and its cofactor GroES are highly conserved, and are required for the folding of many proteins. 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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Triphosphatases - chemistry Cell Proliferation Chaperonin Chaperonin 60 - chemistry Chaperonins - chemistry Circular Dichroism Cpn60 Escherichia coli Escherichia coli - metabolism GroEL In Vitro Techniques Kinetics L-Lactate Dehydrogenase - chemistry L-Lactate Dehydrogenase - metabolism Protein Denaturation Protein Folding Rhizobium leguminosarum Rhizobium leguminosarum - metabolism Temperature |
| title | Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties |
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