Thermoprotective properties of small heat shock proteins from rice, tomato and Synechocystis sp. PCC6803 overexpressed in, and isolated from, Escherichia coli
The present study forms part of a program investigating the role of small heat shock proteins (sHSPs) in the acquired and transgenic thermotolerance of the cyanobacterium Synechococcus PCC7942. The genes for three minimally related sHSPs, OsHSP from Oryza sativacytoplasm, tom111 from Lycopersicon es...
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| Veröffentlicht in: | Australian journal of plant physiology 2001, Vol.28 (12), p.1219-1229 |
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| container_title | Australian journal of plant physiology |
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| creator | PIKE, Carl S GRIEVE, Joanne BADGER, Murray R PRICE, G. Dean |
| description | The present study forms part of a program investigating the role of small heat
shock proteins (sHSPs) in the acquired and transgenic thermotolerance of the
cyanobacterium Synechococcus PCC7942. The genes for
three minimally related sHSPs, OsHSP from
Oryza sativacytoplasm, tom111 from
Lycopersicon esculentumchloroplasts, and 6803 HSP from
Synechocystis sp. PCC6803, were cloned into the
Escherichia coli vector pTrcHisA, so as to produce an
N-terminal polyhistidine tag. The genes were transformed into
E. coli and overexpressed. The tagged HSPs were purified
(not completely in the case of tom111) by immobilised metal affinity
chromatography. The native proteins exhibited a high degree of oligomerisation
when analysed by size-exclusion chromatography. All three proteins were able
to protect malate dehydrogenase (MDH) from in vitro
thermal aggregation. They could also protect several soluble proteins in
E. coli extracts from thermal aggregation
in vitro, as well as protecting phycocyanin in extracts
from Synechococcus sp. PCC7942. None of the proteins
were able to protect photosystem II (measured as ΦPSII, the effective
quantum fluorescence yield of PSII) of thylakoids isolated from
Synechococcus sp. PCC7942 from heat damage
in vitro, although in vivo, after
acclimation, photosystem II did exhibit acquired thermotolerance. |
| doi_str_mv | 10.1071/pp01107 |
| format | Article |
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shock proteins (sHSPs) in the acquired and transgenic thermotolerance of the
cyanobacterium Synechococcus PCC7942. The genes for
three minimally related sHSPs, OsHSP from
Oryza sativacytoplasm, tom111 from
Lycopersicon esculentumchloroplasts, and 6803 HSP from
Synechocystis sp. PCC6803, were cloned into the
Escherichia coli vector pTrcHisA, so as to produce an
N-terminal polyhistidine tag. The genes were transformed into
E. coli and overexpressed. The tagged HSPs were purified
(not completely in the case of tom111) by immobilised metal affinity
chromatography. The native proteins exhibited a high degree of oligomerisation
when analysed by size-exclusion chromatography. All three proteins were able
to protect malate dehydrogenase (MDH) from in vitro
thermal aggregation. They could also protect several soluble proteins in
E. coli extracts from thermal aggregation
in vitro, as well as protecting phycocyanin in extracts
from Synechococcus sp. PCC7942. None of the proteins
were able to protect photosystem II (measured as ΦPSII, the effective
quantum fluorescence yield of PSII) of thylakoids isolated from
Synechococcus sp. PCC7942 from heat damage
in vitro, although in vivo, after
acclimation, photosystem II did exhibit acquired thermotolerance.</description><identifier>ISSN: 0310-7841</identifier><identifier>ISSN: 1445-4408</identifier><identifier>EISSN: 1446-5655</identifier><identifier>DOI: 10.1071/pp01107</identifier><identifier>CODEN: AJPPCH</identifier><language>eng</language><publisher>Collingwood: Commonwealth Scientific and Industrial Research Organization</publisher><subject>Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Physical agents ; Plant physiology and development ; Vegetative apparatus, growth and morphogenesis. Senescence</subject><ispartof>Australian journal of plant physiology, 2001, Vol.28 (12), p.1219-1229</ispartof><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,3339,4012,27910,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13436189$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>PIKE, Carl S</creatorcontrib><creatorcontrib>GRIEVE, Joanne</creatorcontrib><creatorcontrib>BADGER, Murray R</creatorcontrib><creatorcontrib>PRICE, G. Dean</creatorcontrib><title>Thermoprotective properties of small heat shock proteins from rice, tomato and Synechocystis sp. PCC6803 overexpressed in, and isolated from, Escherichia coli</title><title>Australian journal of plant physiology</title><description>The present study forms part of a program investigating the role of small heat
shock proteins (sHSPs) in the acquired and transgenic thermotolerance of the
cyanobacterium Synechococcus PCC7942. The genes for
three minimally related sHSPs, OsHSP from
Oryza sativacytoplasm, tom111 from
Lycopersicon esculentumchloroplasts, and 6803 HSP from
Synechocystis sp. PCC6803, were cloned into the
Escherichia coli vector pTrcHisA, so as to produce an
N-terminal polyhistidine tag. The genes were transformed into
E. coli and overexpressed. The tagged HSPs were purified
(not completely in the case of tom111) by immobilised metal affinity
chromatography. The native proteins exhibited a high degree of oligomerisation
when analysed by size-exclusion chromatography. All three proteins were able
to protect malate dehydrogenase (MDH) from in vitro
thermal aggregation. They could also protect several soluble proteins in
E. coli extracts from thermal aggregation
in vitro, as well as protecting phycocyanin in extracts
from Synechococcus sp. PCC7942. None of the proteins
were able to protect photosystem II (measured as ΦPSII, the effective
quantum fluorescence yield of PSII) of thylakoids isolated from
Synechococcus sp. PCC7942 from heat damage
in vitro, although in vivo, after
acclimation, photosystem II did exhibit acquired thermotolerance.</description><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Physical agents</subject><subject>Plant physiology and development</subject><subject>Vegetative apparatus, growth and morphogenesis. Senescence</subject><issn>0310-7841</issn><issn>1445-4408</issn><issn>1446-5655</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNpFkN1KAzEQhYMoWKv4CnMj3nRrstnsz6WU-gMFC9brkmYnNLq7WTKh2JfxWd22gnBgDsPH4XAYuxV8KnghHvqei8GcsZHIsjxRuVLnbMSl4ElRZuKSXRF9cp7yoshG7Ge1xdD6PviIJrodwmB7DNEhgbdArW4a2KKOQFtvvuBIuo7ABt9CcAYnEH2rowfd1fC-79AM4J6iI6B-CsvZLC-5BL_DgN99QCKswXWTI-_INzoOj0PcBOZkhj7ObJ0G4xt3zS6sbghv_u6YfTzNV7OXZPH2_Dp7XCQmFSomaS03WWVtWVd1lWNepVLqapPVild1mmklldClsFKUgvPSFrlBVQ1SeYGaazlm96dcEzxRQLvug2t12K8FXx9mXS-Xx1kH8u5E9pqMbmzQnXH0j8tM5qKs5C84dXku</recordid><startdate>2001</startdate><enddate>2001</enddate><creator>PIKE, Carl S</creator><creator>GRIEVE, Joanne</creator><creator>BADGER, Murray R</creator><creator>PRICE, G. Dean</creator><general>Commonwealth Scientific and Industrial Research Organization</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>2001</creationdate><title>Thermoprotective properties of small heat shock proteins from rice, tomato and Synechocystis sp. PCC6803 overexpressed in, and isolated from, Escherichia coli</title><author>PIKE, Carl S ; GRIEVE, Joanne ; BADGER, Murray R ; PRICE, G. Dean</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c215t-2d3b49ff8d9d96e69233a9b4d509d24a5351a81f3181008f76ce59e59567ea0a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Physical agents</topic><topic>Plant physiology and development</topic><topic>Vegetative apparatus, growth and morphogenesis. Senescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>PIKE, Carl S</creatorcontrib><creatorcontrib>GRIEVE, Joanne</creatorcontrib><creatorcontrib>BADGER, Murray R</creatorcontrib><creatorcontrib>PRICE, G. Dean</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Australian journal of plant physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>PIKE, Carl S</au><au>GRIEVE, Joanne</au><au>BADGER, Murray R</au><au>PRICE, G. Dean</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermoprotective properties of small heat shock proteins from rice, tomato and Synechocystis sp. PCC6803 overexpressed in, and isolated from, Escherichia coli</atitle><jtitle>Australian journal of plant physiology</jtitle><date>2001</date><risdate>2001</risdate><volume>28</volume><issue>12</issue><spage>1219</spage><epage>1229</epage><pages>1219-1229</pages><issn>0310-7841</issn><issn>1445-4408</issn><eissn>1446-5655</eissn><coden>AJPPCH</coden><abstract>The present study forms part of a program investigating the role of small heat
shock proteins (sHSPs) in the acquired and transgenic thermotolerance of the
cyanobacterium Synechococcus PCC7942. The genes for
three minimally related sHSPs, OsHSP from
Oryza sativacytoplasm, tom111 from
Lycopersicon esculentumchloroplasts, and 6803 HSP from
Synechocystis sp. PCC6803, were cloned into the
Escherichia coli vector pTrcHisA, so as to produce an
N-terminal polyhistidine tag. The genes were transformed into
E. coli and overexpressed. The tagged HSPs were purified
(not completely in the case of tom111) by immobilised metal affinity
chromatography. The native proteins exhibited a high degree of oligomerisation
when analysed by size-exclusion chromatography. All three proteins were able
to protect malate dehydrogenase (MDH) from in vitro
thermal aggregation. They could also protect several soluble proteins in
E. coli extracts from thermal aggregation
in vitro, as well as protecting phycocyanin in extracts
from Synechococcus sp. PCC7942. None of the proteins
were able to protect photosystem II (measured as ΦPSII, the effective
quantum fluorescence yield of PSII) of thylakoids isolated from
Synechococcus sp. PCC7942 from heat damage
in vitro, although in vivo, after
acclimation, photosystem II did exhibit acquired thermotolerance.</abstract><cop>Collingwood</cop><pub>Commonwealth Scientific and Industrial Research Organization</pub><doi>10.1071/pp01107</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0310-7841 |
| ispartof | Australian journal of plant physiology, 2001, Vol.28 (12), p.1219-1229 |
| issn | 0310-7841 1445-4408 1446-5655 |
| language | eng |
| recordid | cdi_crossref_primary_10_1071_PP01107 |
| source | CSIRO Publishing Journals; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Fundamental and applied biological sciences. Psychology Physical agents Plant physiology and development Vegetative apparatus, growth and morphogenesis. Senescence |
| title | Thermoprotective properties of small heat shock proteins from rice, tomato and Synechocystis sp. PCC6803 overexpressed in, and isolated from, Escherichia coli |
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